What is Ergocalciferol used for?

Ergocalciferol is a form of vitamin D, also called vitamin D2. It is marketed under various names including Deltalin (Eli Lilly and Company), Drisdol (Sanofi-Synthelabo) and Calcidol (Patrin Pharma). It is created from viosterol, which in turn is created when ultraviolet light activates ergosterol (which is found in fungi and named as a sterol from ergot) and so comes only from fungi.
Ergocalciferol is widely used as a Vitamin D supplement, and a 2011 clinical guideline considers it to be as effective as cholecalciferol (Vitamin D3), which is produced naturally by the skin when it is exposed to ultraviolet light. However there is now conflicting evidence regarding how similarly D2 and D3 behave in the body and whether they are equally potent. Some studies suggest D3 is more potent, but others have found that they are equally effective.
Ergocalciferol is used for:
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Treating low parathyroid hormone levels, rickets (a vitamin D deficiency condition), and low phosphate levels in the body. It may also be used for other conditions as determined by your doctor.
Ergocalciferol is a form of vitamin D. It works by promoting proper absorption and use of calcium and phosphate in the body and helping to regulate parathyroid hormone levels.
Ergocalciferol (ergocalciferol) is a white, colorless crystal, insoluble in water, soluble in organic solvents, and slightly soluble in vegetable oils.
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PWhat is IP2 (Phosphatidylinositol-4,5-bisphosphate) Monoclonal Antibody?

PIP2 (Phosphatidylinositol-4,5-bisphosphate) Monoclonal Antibody
Specification:100 µg
Purification:Protein G Affinity
Immunogen:PIP2 from bovine spinal cord
species: Species Independent
Applications: ELISA, Immunocytochemistry
Description of PIP2 (Phosphatidylinositol-4,5-bisphosphate) Monoclonal Antibody
Metabolism of inositol phospholipids by intracellular signaling mediators is fundamental to signal transduction in eukaryotic cells. PI-4,5-P2 (PIP2) can be synthesized by phosphorylation of PI-4-P by type I phosphatidylinositol phosphate kinase (PIP5K I), or phosphorylation of PI-5-P by type II PIPK (PIP4K II). PI-4,5-P2 regulation of cellular calcium levels involves its hydrolysis by Phospholipase C (PLC) to produce inositol 1,4,5-triphosphate (IP3) and diacylglycerol (DAG), which serve as second messengers in the import of calcium via IP3-sensitive ion channels and in the activation of PKC, respectively.
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What is Heme iron?

Heme iron (American English) or haem (British English) is a prosthetic group that consists of an iron atom contained in the center of a large heterocyclic organic ring called a porphyrin. Not all porphyrins contain iron, but a substantial fraction of porphyrin-containing metalloproteins have heme as their prosthetic group; these are known as hemoproteins. Hemes are most commonly recognized in their presence as components of hemoglobin, the red pigment in blood, but they are also components of a number of other hemoproteins.
Function of Heme iron
Hemoproteins have diverse biological functions including the transportation of diatomic gases, chemical catalysis, diatomic gas detection, and electron transfer. The heme iron serves as a source or sink of electrons during electron transfer or redox chemistry. In peroxidase reactions, the porphyrin molecule also serves as an electron source. In the transportation or detection of diatomic gases, the gas binds to the heme iron. During the detection of diatomic gases, the binding of the gas ligand to the heme iron induces conformational changes in the surrounding protein.
It has been speculated that the original evolutionary function of hemoproteins was electron transfer in primitive sulfur-based photosynthesis pathways in ancestral cyanobacteria before the appearance of molecular oxygen.
Hemoproteins achieve their remarkable functional diversity by modifying the environment of the heme macrocycle within the protein matrix. For example, the ability of hemoglobin to effectively deliver oxygen to tissues is due to specific amino acid residues located near the heme molecule. Hemoglobin binds oxygen in the pulmonary vasculature, where the pH is high and the pCO2 is low, and releases it in the tissues, where the situations are reversed. This phenomenon is known as the Bohr effect. The molecular mechanism behind this effect is the steric organization of the globin chain; a histidine residue, located adjacent to the heme group, becomes positively charged under acid (low pH) circumstances (which are caused by dissolved CO2 in working muscles, etc.), sterically releasing oxygen from the heme group.
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Where to buy VASP (phospho-Ser239) Monoclonal Antibody (22E11)?

Purification:Thiophilic adsorption and size exclusion chromatography
Immunogen:Synthetic phospho-peptide derived from the sequence of VASP, conjugated to hemocyanin
Description of VASP (phospho-Ser239) Monoclonal Antibody (22E11)
Save 40%.Pricing above includes discount. Offer expires June 30, 2010, or until supplies last.
VASP (vasodilator stimulated phosphoprotein) plays an important role as a substrate in cGMP and cAMP Protein kinase signaling pathways. VASP is ubiquitously expressed, with particularly high concentrations found in thrombocytes, vascular smooth muscle cells, and fibroblasts. In cultured cells VASP is associated with focal contacts, cell-cell contacts, microfilaments and dynamic membrane regions such as the leading edge.
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Benefits of Phosphorylase kinase gamma PHKG2 Monoclonal Antibody 2D12

Phosphorylase kinase gamma PHKG2 Monoclonal Antibody 2D12
Species Reactivity:H
Isotype:IgG2a kappa
Clone:2D12
Host: Mouse
Specification:50 µg
Applications:ELISA, S-ELISA, WB-Re
Immunogen:Mouse monoclonal antibody raised against a full length recombinant PHKG2.
Sequence
MTLDVGPEDELPDWAAAKEFYQKYDPKDVIGRGVSSVVRRCVHRATGHEFAVKIMEVTAERLSPEQLEEVREATRRETHILRQVAGHPHIITLIDSYESSSFMFLVFDLMRKGELFDYLTEKVALSEKETRSIMRSLLEAVSFLHANNIVHRDLKPENILLDDNMQIRLSDFGFSCHLEPGEKLRELCGTPGYLAPEILKCSMDETHPGYGKEVDLWACGVILFTLLAGSPPFWHRRQILMLRMIMEGQYQFSSPEWDDRSSTVKDLISRLLQVDPEARLTAEQALQHPFFERCEGSQPWNLTPRQRFRVAVWTVLAAGRVALSTHRVRPLTKNALLRDPYALRSVRHLIDNCAFRLYGHWVKKGEQQNRAALFQHRPPGPFPIMGPEEEGDSAAITEDEAVLVLG
Mouse monoclonal antibody raised against a full length recombinant PHKG2.
Benefits of Phosphorylase kinase gamma PHKG2 Monoclonal Antibody 2D12
Antibody Bioguarantee
Evaluate our antibodies with complete peace of mind. If the antibody does not perform in your application, we will issue a full credit or replacement antibody. phospho antibody
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What is Vitamin D3 1.0 mio.I.U./g kosher?

Vitamin D3 is both a vitamin and a hormone. It acts as a vitamin when it binds with calcium for proper absorption. Humans cannot digest calcium without adequate amounts of Vitamin D3.
Vitamin D is a group of fat-soluble secosteroids. In humans, vitamin D is unique both because it functions as a prohormone and because the body can synthesize it (as vitamin D3) when sun exposure is adequate.
Vitamin D3 is found in many dietary sources, such as fish, eggs, fortified milk, and cod liver oil. The sun also contributes significantly to the daily production of vitamin D, and as little as 10 minutes of exposure is thought to be enough to prevent deficiencies. The term "vitamin D" refers to several different forms of this vitamin. Two forms are important in humans: ergocalciferol (vitamin D2) and cholecalciferol (vitamin D3). Vitamin D2 is synthesized by plants. Vitamin D3 is synthesized by humans in the skin when it is exposed to ultraviolet B (UVB) rays from sunlight. Foods may be fortified with vitamin D2 or D3.
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PIP2 (Phosphatidylinositol-4,5-bisphosphate) Monoclonal Antibody

Description of PIP2 (Phosphatidylinositol-4,5-bisphosphate) Monoclonal Antibody
Phosphatidylinositol-4,5-bisphophate (PIP2) controls TRPM6 activation and Mg2+ influx. Stimulation of PLC-coupled M1-receptors to deplete PIP2 potently inactivates TRPM6. Translocation of over-expressed 5-phosphatase to cell membrane to specifically hydrolyze PIP2 also completely inhibits TRPM6. Moreover, depolarization-induced-activation of the voltage-sensitive-phosphatase (Ci-VSP) simultaneously depletes PIP2 and inhibits TRPM6. PLC-activation induced PIP2-depletion not only inhibits TRPM6, but also abolishes TRPM6-mediated Mg2+ influx.
Applications: ELISA, Immunocytochemistry
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Uses of Panthenol

Panthenol is the alcohol analog of pantothenic acid (vitamin B5), and is thus a provitamin of B5. In organisms it is quickly oxidized to pantothenate. Panthenol is a highly viscous transparent liquid at room temperature, but salts of pantothenic acid (for example sodium pantothenate) are powders (typically white). It is soluble in water, alcohol and propylene glycol, soluble in ether and chloroform, and slightly soluble in glycerin.
Uses
Because panthenol binds well to hair follicles, and attracts moisture from the air, it is a moisturizing agent used in shampoos and conditioners. It lubricates the hair without feeling greasy. It smoothes roughened hair surfaces, making them shiny and easier to comb.
In cosmetics, panthenol is a humectant, emollient and moisturizer. It binds to the hair shaft readily and is a frequent component of shampoos and hair conditioners (in concentrations of 0.1-1%). It coats the hair and seals its surface, lubricating the hair shaft and making strands appear shiny. It is also recommended by many tattoo artists as a moisturising cream for new tattoos.
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Where to buy PKC gamma (phospho-Thr514) Polyclonal Antibody?

PKC is an 80 kDa member of the conventional group (cPKCs: sensitive to calcium, diacylglycerol and phorbol esters) of the PKC family of serine/threonine family kinases that are involved in a wide range of physiological processes including mitogenesis, cell survival and transcriptional regulation. PKC plays a key role in neuronal signal transduction and is translocated from the nucleus to the cytoplasm upon activation by phorbol ester, where in epithelial cells it has been implicated in regulating intracellular communication. The activation loop threonine (threonine 514 in PKC of conventional PKCs is phosphorylated by phosphoinositide-dependent kinase-1 (PDK1), which is necessary for their autophosphorylation, a critical step in the generation of a catalytically mature enzyme.
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Description of Protein phosphatase PPP3CC Recombinant Protein

Description of Protein phosphatase PPP3CC Recombinant Protein
Calmodulin-dependent protein phosphatase, calcineurin, is involved in a wide range of biologic activities, acting as a Ca(2+)-dependent modifier of phosphorylation status. In testis, the motility of the sperm is thought to be controlled by cAMP-dependent phosphorylation and a unique form of calcineurin appears to be associated with the flagellum. The calcineurin holoenzyme is composed of catalytic and regulatory subunits of 60 and 18 kD, respectively. At least 3 genes, calcineurin A-alpha (CALNA1; MIM 114105), calcineurin A-beta (CALNA2; MIM 114106), and calcineurin A-gamma (CALNA3), have been cloned for the catalytic subunit. These genes have been identified in humans, mice, and rats, and are highly conserved between species (90 to 95% amino acid identity).
Uses:Useful in Western Blot and ELISA. This protein has not been tested for any functionality. This product may contain endotoxins and is not suitable for use with live cells.
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Where to buy Nicotinamide?

Nicotinamide, also known as niacinamide and nicotinic acid amide, is the amide of nicotinic acid (vitamin B3 / niacin). Nicotinamide is a water-soluble vitamin and is part of the vitamin B group. Nicotinic acid, also known as niacin, is converted to nicotinamide in vivo, and, though the two are identical in their vitamin functions, nicotinamide does not have the same pharmacologic and toxic effects of niacin, which occur incidental to niacin's conversion. Thus nicotinamide does not reduce cholesterol or cause flushing,[1] although nicotinamide may be toxic to the liver at doses exceeding 3 g/day for adults.[2] In cells, niacin is incorporated into nicotinamide adenine dinucleotide (NAD) and nicotinamide adenine dinucleotide phosphate (NADP), although the pathways for nicotinamide and nicotinic acid are very similar. NAD+ and NADP+ are coenzymes in a wide variety of enzymatic oxidation-reduction reactions.
Use
Nicotinamide has demonstrated anti-inflammatory actions that may be of benefit to patients with inflammatory skin conditions.[4] These conditions include acne vulgaris, and the compound can suppress antigen-induced, lymphocytic transformation and inhibit 3'-5' cyclic AMP phosphodiesterase. Nicotinamide has demonstrated the ability to block the inflammatory actions of iodides known to precipitate or exacerbate inflammatory acne.
Nicomide is the name of an acne medication and, in its vitamin supplement form, the most predominant ingredient is 750 mg of nicotinamide, based on this area of research. Also, it is used topically as a 4% or 5% gel or cream - as effective as topical 1% clindamycin (8-week double-blind trial) performed at the New York University College of Medicine. Nicotinamide acne treatment is also available as Nicotinamide pads and cream.
Nicotinamide lacks the vasodilator, gastrointestinal, hepatic, and hypolipidemic actions of nicotinic acid. As such, nicotinamide has not been shown to produce the flushing, itching, and burning sensations of the skin as is commonly seen when large doses of nicotinic acid are administered orally. High-dose nicotinamide should still, however, be considered as a drug with toxic potential at adult doses in excess of 3 g/day and unsupervised use should be discouraged. In overall, it rarely causes side effects, and is considered generally safe as a food additive, and as a component in cosmetics and medication.
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Where to buy Akt (PKB) Kinase Activity Kit?

Akt (PKB) Kinase Activity Kit is a non-radioactive Akt kinase activity assay, providing a safe, rapid and reliable method for the screening of inhibitors or activators of Akt and for quantitating the activity of Akt in purified or partially purified enzyme preparations. The Akt Kinase activity kit is based on a solid phase enzyme immunoassay (EIA) that utilizes a specific synthetic peptide as a substrate for Akt and a polyclonal antibody that recognizes the phosphorylated form of the substrate. The assay is designed for the analysis of Akt (1, 2, 3) activity in the solution phase.
Application: For the measurement of Akt in partially purified, purified, or crude enzyme preparations from any species.
Use/Stability:Store all components at +4°, except active kinase at -80°.

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Where to buy Von Willebrand factor?

Von Willebrand factor (vWF) is a blood glycoprotein involved in hemostasis. It is deficient or defective in von Willebrand disease and is involved in a large number of other diseases, including thrombotic thrombocytopenic purpura, Heyde's syndrome, and possibly hemolytic-uremic syndrome.[1] Increased plasma levels in a large number of cardiovascular, neoplastic and connective tissue diseases are presumed to arise from adverse changes to the endothelium, and may contribute to an increased risk of thrombosis.
Synthesis
Von Willebrand factor is a large multimeric glycoprotein present in blood plasma and produced constitutively in endothelium (in the Weibel-Palade bodies), megakaryocytes (α-granules of platelets), and subendothelial connective tissue.
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Descriptions of Potassium formate

Description:
Potassium formate is the potassium salt of formic acid. It is an intermediate in the formate potash process for the production of potassium.[2] Potassium formate has also been studied as a potential environmentally-friendly deicing salt for use on roads.
Application: Potassium formate are mainly used for Drilling Fluids and Completion Fluids in oil and gas industry, also used in leather industry, printing and dyeing industry, cement industry and other relatively industries.
Appearance: Potassium Formate is colorless and semi transparent liquid.
Packing:  Potassium Formate to be packed in 25 kgs plastic woven sacks.
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Applications of PKA Kinase Activity Kit

PKA Kinase Activity Kit is an efficient assay that utilizes little sample volume.
Application: For the quantitative determination of PKA kinase activity in partially purified, purified, or crude enzyme preparations from any species.
Use/Stability: Store all components at +4°, except active kinase at -80°.
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What is 5-Bromonicotinic acid?

5-Bromonicotinic acid is white to light yellow crystalline powder. It is used as pharmaceutical intermediates.
SYNONYMS: 5-Bromo-3-pyridinecarboxylic acid; 5-Bromoniacin;
5-Bromopyridine-3-carboxylic acid;
5-Bromonicotinic acid is used as an intermediate for agrochemcials, feed additives, pharmaceuticals and animal food enrichments.
STABILITY: Stable under ordinary conditions
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Where to find v-Akt phospho-Tyr326 AKT1 Polyclonal Antibody A?

Description of v-Akt phospho-Tyr326 AKT1 Polyclonal Antibody A
The serine-threonine protein kinase encoded by the AKT1 gene is catalytically inactive in serum-starved primary and immortalized fibroblasts. AKT1 and the related AKT2 are activated by platelet-derived growth factor. The activation is rapid and specific, and it is abrogated by mutations in the pleckstrin homology domain of AKT1. It was shown that the activation occurs through phosphatidylinositol 3-kinase.
In the developing nervous system AKT is a critical mediator of growth factor-induced neuronal survival. Survival factors can suppress apoptosis in a transcription-independent manner by activating the serine/threonine kinase AKT1, which then phosphorylates and inactivates components of the apoptotic machinery. Multiple alternatively spliced transcript variants have been found for this gene.
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Are you searching Coronin?

Coronin is an actin binding protein which also interacts with microtubules and in some cell types is associated with phagocytosis. Coronin proteins are expressed in a large number of eukaryotic organisms from yeast to man.
Function
Yeast Coronin Crn1 and Drosophila Dpod1 were found crosslink actin and microtubule cytoskeleton. C.elegans POD-1 and Drosophila Coronin homologue regulate actin cytoskeleton and are involved in vesicular trafficking.
Seven different isoforms of Coronin have been reported in mammals. The most well studied isoforms are Coronin 1 (Coronin 1A) and Coronin 1B. Coronin 1 exerted an inhibitory effect on cellular steady-state F-actin formation via an Arp2/3-dependent mechanism.
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What is Kinase insert domain Receptor Polyclonal Antibody 2?

Kinase insert domain Receptor  Polyclonal Antibody 2 applies in human species.It  come from rabbit.It is used in immunohistochemical, immune imprinting and enzyme-linked immunosorbent.
Applications:ELISA, IHC-P, WB-Ce                                
Immunogen:Rabbit polyclonal antibody raised against synthetic phosphopeptides of KDR.
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How to Use FAK (phospho-Tyr397) Polyclonal Antibody

FAK, Focal adhesion kinase, is a 125 kDa non-receptor protein tyrosine kinase that is a substrate for Src and a key element in growth factor and integrin signaling. FAK plays a central role in cell spreading, differentiation, migration, cell death, and acceleration of the G1 to reciprocal ohm phase angle transition of the cell cycle. Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Tyr397 of human FAK. Antibodies are purified by protein A and peptide affinity chromatography.

The antiserum was produced against a chemically synthesized phosphopeptide derived from the region of FAK that contains tyrosine 397. The sequence is conserved in human, mouse, rat, chicken and frog.

The antibody has been purified from rabbit serum by sequential epitope-specific chromatography. The antibody has been negatively preadsorbed using a non-phosphopeptide corresponding to the site of phosphorylation to remove antibody that is reactive with non-phosphorylated FAK. The net merchandise constitutes brought forth by affinity chromatography using a FAK-derived peptide that is phosphorylated at tyrosine 397.

Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.

Synthetic peptide derived from the region of Focal Adhesion Kinase that contains tyrosine 397. The sequence is conserved in human, mouse, rat, chicken and frog.

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The Application of Factor XIII

Factor XIII is a transglutaminase that circulates in the plasma as a heterotetramer of two catalytic A subunits and two carrier B subunits. When thrombin has converted fibrinogen to fibrin, the latter forms a proteinaceous network in which every E-unit is crosslinked to only one D-unit. When someone births a insufficiency of Factor XIII, the tenuously formed clot will eventually break down and cause recurrent bleeds.  The prolonged bleeding that is associated with Factor XIII constitutes usually connected with trauma. Among severe patients there is a high risk of head bleeds with or without trauma. Bleeding immediately after surgery is usually not excessive, but can be stayed.  Charwomen who belong untreated danger spontaneous abortion.

Factor XIII is activated by thrombin into factor XIIIa; its activation into Factor XIIIa requires calcium every bit a cofactor. A cleavage by thrombin between residue Arg37 and Gly38 on the N-terminus of the A subunit, leads to the departure of the activation peptide (MW 4000 da). In the presence of calcium the carrier subunits dissociate from the catalytic subunits, leading to a 3D change in conformation of factor XIII and hence the exposure of catalytic cysteine residue. Upon activation by thrombin, divisor XIIIa dissembles on duty fibrin to form γ-glutamyl-Є-lysyl amide cross links between fibrin corpuscles to form an insoluble clot.

There have been more than 60 FXIII mutations identified in the current literature. In addition, single nucleotide polymorphisms have been described, some of which have been shown to affect FXIII activity, contributing further to the heterogeneity in patient presentation and severity of clinical symptoms. Although there is a lifelong risk of bleeding, the prognosis is excellent when current prophylactic treatment is available using cryoprecipitate or plasma-derived FXIII contract.

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What is Riboflavin Used for

Riboflavin, also known as vitamin B2 is an easily absorbed micronutrient with a key role in maintaining health in humans and animals. It is the central component of the cofactors FAD and FMN, and is therefore required by all flavoproteins. The name "riboflavin" comes from "ribose" (the sugar whose reduced form, ribitol, forms part of its structure) and "flavin", the ring-moiety which imparts the yellow color to the oxidized molecule (from Latin flavus, "yellow"). The abridged class, which goes on fashionable metabolism along with the oxidized configuration, is blanched. Dineros and cereals are often fortified with riboflavin. Fortified means the vitamin has been added to the food.

As such, vitamin B2 costs compulsory for a all-encompassing diverseness of cellular processes. It plays a key role in energy metabolism, and for the metabolism of fats, ketone bodies, carbohydrates, and proteins. It is also used as an orange-red food colour additive, designated in Europe as the tocopherol issue E101, Coenzymes descended from riboflavin are termed flavocoenzymes, and enzymes that use a flavocoenzyme are called flavoproteins.

The glutathione redox cycle plays a major role in protecting organisms from reactive oxygen species, such as hydroperoxides. Glutathione reductase requires FAD to regenerate two molecules of reduced glutathione from oxidized glutathione. Riboflavin deficiency delivers been consociated with expanded oxidative stress.

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How to Use Serum albumin

Serum albumin, often referred to simply as albumin is a protein that in humans is encoded by the ALB gene.

Albumin is synthesized in the liver as preproalbumin, which has an N-terminal peptide that is removed before the nascent protein is released from the rough endoplasmic reticulum. The product, proalbumin, is in turn cleaved in the Golgi vesicles to produce the secreted albumin.

Serum albumin is the most abundant plasma protein in mammals. The gene for albumin is located on chromosome 4 and mutations in this gene can result in anomalous proteins. The human albumin gene is 16,961 nucleotides long from the putative 'cap' site to the first poly(A) addition site. It is split into 15 exons that are symmetrically placed within the 3 domains thought to have arisen by triplication of a single primordial domain.

Albumin is essential for maintaining the osmotic pressure needed for proper distribution of body fluids between intravascular compartments and body tissues. It also acts as a plasma carrier by non-specifically binding several hydrophobic steroid hormones and as a transport protein for hemin and fatty acids. Too much serum albumin in the body can be harmful.

Albumin transports hormones, fatty acids, and other compounds, buffers pH, and maintains osmotic pressure, among other functions.

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What is Calcium Pidolate Used for

Calcium pidolate is a safe and efficient treatment for osteoporosis because of easy absorption, which is very helpful in maintaining the calcium balance.

Calcium Pidolate is a remarkably soluble salt which remains soluble across a broad spectrum of pH. Fashionable combination with Pidolic bitter, which is a composing element of the collagen matrices, it can play a double role in reinforcing the skeletal system and the brooking tissue. It is found in many proteins including bacteriorhodopsin. N-terminal glutamine residues can spontaneously cyclize to become pyroglutamate. This is one of several forms of blocked N-terminals which present a problem for N-terminal sequencing using Edman chemistry, which requires a free primary amino group not present in pyroglutamic acid.

This can be again converted back to Calcium carbonate, by blowing Carbon dioxide through the solution. The white precipitate is Calcium carbonate:

Ca(OH)2 + CO2 ----> CaCO3 + H2O.c

The bioavailability of Calcium Pidolate has been established by many scientific and clinical tests.

Store in a well-closed container at a temperature not exceeding 25°C, protected from direct sunlight and Moisture, unless otherwise specified.

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