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Name :
FGFR3 Human, HisDescription:
Fibroblast Growth Factor Receptor-3 Human Recombinant, His Tag
CD333 Antigen, HSFGFR3EX, EC 2.7.10, CD333, CEK2, ACH, Fibroblast Growth Factor Receptor 3, EC 2.7.10.1, FGFR-3, JTK4, Fibroblast Growth Factor Receptor 3 Variant 4, Achondroplasia, Thanatophoric Dwarfism, Hydroxyaryl-Protein Kinase, Tyrosine Kinase JTK4.
Product # :
PKA-101Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
FGFR3 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 592 amino acids (23-375a.a.) and having a molecular mass of 65.1kDa (Molecular size on SDS-PAGE will appear at approximately 70-100kDa). FGFR3 is expressed with a 239 amino acid hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
FGFR3 protein solution (1mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Fibroblast Growth Factors (FGFs) comprise a family of at least eighteen structurally realted proteins that are involved in a multitude of physiological and pathological cellular processes, including cell growth, differentation, angiogenesis, wound healing and tumorgenesis. The biological activities of the FGFs are mediated by a family if type I transmembrane tyrosine kinases which undergo dimerization and autophosphorylation after ligand binding. Four distinct genes encoding closely related FGF receptors, FGFR-1to -4 are known. Multiple forms of FGFR-1 to -3 are generated by alternative splicing of the mRNAs. A frequent splicing event involving FGFR-1 and -2 results in receptors containing all three Ig domains, referred to as the alpha isoform, or only IgII and IgIII, referred to as the ? isoform. Only the alpha isoform has been identified for FGFR-3 and FGFR-4. Additional splicing events for FGFR-1 to -3, involving the C-terminal half of the IgIII domain encoded by two mutually exclusive alternative exons, generate FGF receptors with alternative IgIII domains (IIIb and IIIc). A IIIa isoform which is a secreted FGF binding protein containing only the N-terminal half of the IgIII domain plus some intron sequences has also been reported for FGFR-1. Mutations in FGFR-1 to -3 have been found in patients with birth defects involving craniosynostosis.
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Synonyms
CD333 Antigen, HSFGFR3EX, EC 2.7.10, CD333, CEK2, ACH, Fibroblast Growth Factor Receptor 3, EC 2.7.10.1, FGFR-3, JTK4, Fibroblast Growth Factor Receptor 3 Variant 4, Achondroplasia, Thanatophoric Dwarfism, Hydroxyaryl-Protein Kinase, Tyrosine Kinase JTK4.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
ESLGTEQRVV GRAAEVPGPE PGQQEQLVFG SGDAVELSCP PPGGGPMGPT VWVKDGTGLV PSERVLVGPQ RLQVLNASHE DSGAYSCRQR LTQRVLCHFS VRVTDAPSSG DDEDGEDEAE DTGVDTGAPY WTRPERMDKK LLAVPAANTV RFRCPAAGNP TPSISWLKNG REFRGEHRIG GIKLRHQQWS LVMESVVPSD RGNYTCVVEN KFGSIRQTYT LDVLERSPHR PILQAGLPAN QTAVLGSDVE FHCKVYSDAQ PHIQWLKHVE VNGSKVGPDG TPYVTVLKTA GANTTDKELE VLSLHNVTFE DAGEYTCLAG NSIGFSHHSA WLVVLPAEEE LVEADEAGSV YAGLEPKSCD KTHTCPPCPA PELLGGPSVF LFPPKPKDTL MISRTPEVTC VVVDVSHEDP EVKFNWYVDG VEVHNAKTKP REEQYNSTYR VVSVLTVLHQ DWLNGKEYKC KVSNKALPAP IEKTISKAKG QPREPQVYTL PPSRDELTKN QVSLTCLVKG FYPSDIAVEW ESNGQPENNY KTTPPVLDSD GSFFLYSKLT VDKSRWQQGN VFSCSVMHEA LHNHYTQKSL SLSPGKHHHH HH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
GM-CSF RatDescription:
Granulocyte Macrophage-Colony Stimulating Factor Rat Recombinant
CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, Molgramostin, Sargramostim.
Product # :
CYT-395Price :
Quantity :
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Shipped at Room temp
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Description
Granulocyte Macrophage Colony Stimulating Factor Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 128 amino acids and having a molecular mass of 14590.65 Dalton. GM-CSF Rat Recombinant is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GM-CSF Rat was lyophilized with no additives.
Purity
Greater than 96.0% as determined by:
(a)Analysis by RP-HPLC.
(b)Analysis by SDS-PAGE.Biological Activity
The ED50 as calculated by the dose-dependent stimulation of the proliferation of murine FDC-P1 cells is less than 0.01ng/ml, corresponding to a specific activity of > 1×108units/mg.
More Info
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Introduction
GMCSF is a cytokine that controls the production, differentiation, and function of granulocytes and macrophages. The active form of the protein is found extracellularly as a homodimer. This gene has been localized to a cluster of related genes at chromosome region 5q31, which is known to be associated with interstitial deletions in the 5q- syndrome and acute myelogenous leukemia. Other genes in the cluster include those encoding interleukins 4, 5, and 13.
GM-CSF stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes. -
Synonyms
CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, Molgramostin, Sargramostim.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Granulocyte Macrophage Colony Stimulating Factor although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GMCSF should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Granulocyte Macrophage Colony Stimulating Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MAPTRSPNPV TRPWKHVDAI KEALSLLNDM RALENEKNED VDIISNEFSI
QRPTCVQTRL KLYKQGLRGN LTKLNGALTM IASHYQTNCP PTPETDCEIE
VTTFEDFIKN LKGFLFDIPF DCWKPVQK.
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Background
What is the molecular weight/Mw of GM-CSF RAT Protein?
GM-CSF RAT Protein has a total Mw of 14.59kDa.
What is the source or expression system of GM-CSF RAT Protein?
Escherichia Coli.
What is the Purity of GM-CSF RAT Protein?
GM-CSF RAT Protein is >96% pure as determined by SDS-PAGE.
What is the Biological Activity of GM-CSF RAT Protein?
The ED50 as calculated by the dose-dependent stimulation of the proliferation of murine FDC-P1 cells is less than 0.01ng/ml, corresponding to a specific activity of > 1×108units/mg.
What is the amino acid sequence of GM-CSF RAT Protein?
MAPTRSPNPV TRPWKHVDAI KEALSLLNDM RALENEKNED VDIISNEFSI
QRPTCVQTRL KLYKQGLRGN LTKLNGALTM IASHYQTNCP PTPETDCEIE
VTTFEDFIKN LKGFLFDIPF DCWKPVQK.
What applications can GM-CSF RAT Protein be used in?
GM-CSF RAT Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for GM-CSF RAT Protein?
The endotoxin level is minimal, GM-CSF RAT Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
IL 2 Human, YeastDescription:
Interleukin-2 Human Recombinant, Yeast
Interleukin-2, T-cell growth factor (TCGF), Interleukin-2, Lymphokine, IL-2.
Product # :
CYT-797Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Interleukin-2 Human Recombinant produced in yeast is a single, glycosylated polypeptide chain containing 134 amino acids and having a molecular mass of 14 kDa. The IL-2 is purified by proprietary chromatographic techniques.
Source
Pichia pastoris.
Formulation
The protein was lyophilized from a 0.2µm filtered solution in 20mM sodium phosphate buffer pH 7.0 in absence of any carrier protein.
Purity
Greater than 98% as determined by SDS-PAGE.
Biological Activity
The biological activity is determined by the dose dependent proliferation of mouse CTLL–2 cells. Optimal concentration for individual application should be determined by a dose response assay. ED50 range = 0.08–0.5ng/mlMore Info
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Introduction
IL2 is a secreted cytokine that is important for the proliferation of T and B lymphocytes. The receptor of this cytokine is a heterotrimeric protein complex whose gamma chain is also shared by interleukin 4 (IL4) and interleukin 7 (IL7). The expression of this gene in mature thymocytes is monoallelic, which represents an unusual regulatory mode for controlling the precise expression of a single gene. The targeted disruption of a similar gene in mice leads to ulcerative colitis-like disease, which suggests an essential role of this gene in the immune response to antigenic stimuli.
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Synonyms
Interleukin-2, T-cell growth factor (TCGF), Interleukin-2, Lymphokine, IL-2.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Interleukin-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution Interleukin-2 should be stored at 4C between 2-7 days and for future use below -18C. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Interleukin-2 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
A P T S S S T K K T Q L Q L E H L L L D L Q M I L N G I N N Y K N P K L T R M L T F K F Y M P K K A T E L K H L Q C L E E E L K P L E E V L N L A Q S K N F H L R P R D L I S N I N V I V L E L K G S E T T F M C E Y A D E T A T I V E F L N R W I T F C Q S I I S T L T.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
IL 4 Human, YeastDescription:
Interleukin 4 Human Recombinant, Yeast
BCGF, BCDF, B cell stimulating factor, BSF-1, Lymphocyte stimulatory factor 1, IL-4, MGC79402, Binetrakin, Pitrakinra.
Product # :
CYT-712Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Interleukin-4 Human Recombinant produced in yeast is a single, glycosylated polypeptide chain containing 129 amino acids.The IL-4 is purified by proprietary chromatographic techniques.
Source
Pichia pastoris.
Formulation
The protein was lyophilized from 0.2µm filtered solution in 20mM sodium phosphate buffer pH 6.0 in absence of any carrier protein.
Purity
Greater than 98% as determined by SDS-PAGE.
Biological Activity
The biological activity is determined by measuring the dose-dependent proliferation of human TF–1 cells and CD23 expression. A concentration range of 0.1–10.0 ng/ml is effective for most in vitro applications. ED50 = 0.05–0.4ng/ml.More Info
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Introduction
IL4 is a pleiotropic cytokine produced by activated T cells. IL4 is a ligand for interleukin 4 receptor. The interleukin 4 receptor also binds to IL13, which may contribute to many overlapping functions of this cytokine and IL13. STAT6, a signal transducer and activator of transcription, has been shown to play a central role in mediating the immune regulatory signal of this cytokine. This gene, IL3, IL5, IL13, and CSF2 form a cytokine gene cluster on chromosome 5q, with this gene particularly close to IL13. IL4, IL13 and IL5 are found to be regulated coordinately by several long-range regulatory elements in an over 120 kilobase range on the chromosome. Two alternatively spliced transcript variants of this gene encoding distinct isoforms have been reported.
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Synonyms
BCGF, BCDF, B cell stimulating factor, BSF-1, Lymphocyte stimulatory factor 1, IL-4, MGC79402, Binetrakin, Pitrakinra.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Interleukin-4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Interleukin-4 should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Interleukin-4 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
BETV4Description:
Polcalcin Bet v 4 Recombinant
Polcalcin Bet v 4, Calcium-binding pollen allergen Bet v 4, Bet v 4, BETV4.
Product # :
ALR-017Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant BETV4 produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 10,473 Dalton. BETV4 is expressed with a 6xHis tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Sf9 insect cells.
Formulation
BETV4 is supplied in 20mM HEPES buffer pH-7.9 and 6M Urea.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
BETV4 is primarily expressed in mature birch (Betula verrucosa) pollen and Causes an allergic reaction in human. BETV4 is a calcium-binding protein of 2-EF-hand type, which is exists in pollen of various plant species. This cross-reactivity can serve as a marker allergen for plant polysensitization.
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Synonyms
Polcalcin Bet v 4, Calcium-binding pollen allergen Bet v 4, Bet v 4, BETV4.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
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Immunological Functions
1. Binds IgE type human antibodies. 2. Immunodot test with positive/negative sera panels.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Leptin N82K Human, PEGDescription:
Leptin N82K Human Recombinant, Pegylated
OB Protein, Obesity Protein, OBS, Obesity factor.
Product # :
CYT-1107Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Pegylated Leptin N82K Human Recombinant produced in E.Coli is a single non-glycosilated polypeptide chain containing 146 amino acids, an additional Ala at N-terminus and one molecule of PEG 20 kDa at its N-terminus acids and having a molecular weight of 35.6kDa. However due to enlarged hydrodymanic volume it runs on the SDS-PAGE as 48 kDa protein and in gel-filtration on Superdex 200 as over 200 kDa protein. Pegylated Leptin N82K Human Recombinant was purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3 Having 35-40% protein.
Purity
Greater than 99.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.Biological Activity
Pegylated Leptin Human is capable of stimulatng proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Pegylated Leptin in vitro activity is 5-7 fold lower than the non-pegylated recombinant human leptin but in vivo Pegylated Leptin has profound weight reducing effect (as compared to the non-pegylated recombinant human leptin), resulting mainly from reduced food intake.
More Info
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Introduction
Leptin takes an important part in the regulation of energy balance and body weight control.After entering the circulation, Leptin binds LEPRwhich results in the activation of several major signalling pathways. In the hypothalamus Leptin acts as an appetite-regulating factor that induces a decrease in food intake and an increase in energy consumption and also regulates bone mass and secretion of hypothalamo-pituitary-adrenal hormones. In the periphery, increases basal metabolism, regulates pancreatic beta-cell function and insulin secretion and affects innate and adaptive immunity.
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Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Pegylated Leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Pegylated Leptin N82K should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Pegylated Leptin in sterile water or 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
AngiotensinDescription:
Angiotensin
Angiotensinogen, Serpin A8, ANHU, SERPINA8.
Product # :
ENZ-283Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Angiotensin contains a total of 8 amino acids having a molecular weight of 1031.2 Dalton and a molecular formula of C49H70N14O11.
Source
Synthetic.
Purity
Greater than 98.0% as determined by RP-HPLC.
More Info
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Introduction
Angiotensin is an oligopeptide in the blood that causes vasoconstriction, increased blood pressure, and release of aldosterone from the adrenal cortex. It is a powerful dipsogen. It is derived from the precursor molecule angiotensinogen, a serum globulin produced in the liver. It plays an important role in the renin-angiotensin system.
The protein encoded by this gene, pre-angiotensinogen or angiotensinogen precursor, is expressed in the liver and is cleaved by the enzyme renin in response to lowered blood pressure. The resulting product, angiotensin I is then cleaved by angiotensin converting enzyme (ACE) to generate the physiologically active enzyme angiotensin II. The protein is involved in maintaining blood pressure and in the pathogenesis of essential hypertension and preeclampsia. -
Synonyms
Angiotensinogen, Serpin A8, ANHU, SERPINA8.
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Physical Appearance
Sterile Filtered white lyophilized powder.
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Stability
Lyophilized Angiotensin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Serpin A8 should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Angiotensin in sterile 18MΩ-cm H2O not less than 100 µg/ml or more than 10 mg/ml solutions.
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Amino Acid Sequence
Asn-Arg-Val-Tyr-Val-His-Pro-Phe-OH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Thymosin a1 humanDescription:
Thymosin a1 Acetate
Product # :
HOR-243Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Thymosin a1 acetate, also known as thymalfasin has immunoregulatory properties enhancing immune functions. Thymosin a1 has a molecular formula of C129H215N33O55 a.a. sequence of Ac-Ser-Asp-Ala-Ala-Val-Asp-Thr-Ser-Ser-Glu-Ile-Thr-Thr-Lys-Asp-Leu-Lys-Glu-Lys-Lys-Glu-Val-Val-Glu-Glu-Ala-Glu-Asn-OH and having a Mw of 3108.32 Dalton.
Formulation
The protein (1mg/ml) was lyophilized with no additives.
Purity
Greater than 99.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
Thymalfasin is a synthetic analogue of thymosin-alpha-1, a 28-amino acid protein derived from the precursor protein prothymosin-alpha. Exhibiting a variety of immunoregulating properties, thymosin-alpha-1 induces differentiation of murine T-cell precursors and human thymocytes and the terminal differentiation of functionally immature cord blood lymphocytes and induces production of IL-2, high affinity IL-2 receptors, and B-cell growth factors by peripheral blood mononuclear cells. T-helper and cytotoxic/suppressor T-cell populations are targets of thymosin activity. Thymosin-alpha-1 has been shown to increase the efficiency of antigen presentation by macrophages and to be an endogenous modulator of alpha-thrombin activity.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Thymosin a1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Thymalfasin should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Thymosin a1 in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
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Background
What is the molecular weight/Mw of THYMOSIN-A1 HUMAN Protein?
THYMOSIN-A1 HUMAN Protein has a total Mw of 3.1kDa.
What is the Purity of THYMOSIN-A1 HUMAN Protein?
THYMOSIN-A1 HUMAN Protein is >99% pure as determined by SDS-PAGE.
What is the Biological Activity of THYMOSIN-A1 HUMAN Protein?
The biological functionality of THYMOSIN-A1 HUMAN Protein will be determined in the future.
What applications can THYMOSIN-A1 HUMAN Protein be used in?
THYMOSIN-A1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for THYMOSIN-A1 HUMAN Protein?
The endotoxin level is minimal, THYMOSIN-A1 HUMAN Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
UMOD FelineDescription:
Uromodulin Feline
Tamm-Horsfall urinary glycoprotein, THP, FJHN, HNFJ, THGP, MCKD2, ADMCKD2, UMOD, Uromodulin.
Product # :
ENZ-732Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Feline Uromodulin is a 95kDa glycoprotein which is produced in the thick ascending limb of Henle´s loop and early distal convoluted tubules of the nephron.
Source
Feline Urine.
Formulation
The UMOD protein was lyophilized from 0.4µm filtered solution at a concentration of 0.5mg/ml containing deionized water.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Uromodulin is the most abundant protein in normal urine. Its secretion in urine follows proteolytic cleavage of the ectodomain of its glycosyl phosphatidylinosital-anchored counterpart that is situated on the luminal cell surface of the loop of Henle. Uromodulin plays a role as a constitutive inhibitor of calcium crystallization in renal fluids. Secretion of uromodulin in urine provides protection against urinary tract infections caused by uropathogenic bacteria. Defects in Uromodulin expression are associated with the autosomal dominant renal disorders medullary cystic kidney disease-2 (MCKD2) and familial juvenile hyperuricemic nephropathy (FJHN). These disorders are characterized by juvenile onset of hyperuricemia, gout, and progressive renal failure. While several transcript variants may exist for this gene, the full-length natures of only two have been described to date. UMOD is involved in regulating the circulating activity of cytokines as it binds to il-1, il-2 and tnf with high affinity.
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Synonyms
Tamm-Horsfall urinary glycoprotein, THP, FJHN, HNFJ, THGP, MCKD2, ADMCKD2, UMOD, Uromodulin.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
Add deionized water to prepare a working stock solution of approximately 0.5mg/mL and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
GM-CSF PorcineDescription:
Granulocyte Macrophage-Colony Stimulating Factor Porcine Recombinant
CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, Molgramostin, Sargramostim.
Product # :
CYT-1095Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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- source
- formulation
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- biological activity
- More Info
Description
Granulocyte Macrophage-Colony Stimulating Factor Porcine Recombinant produced in E. coli is a non-glycosylated monomer chain containing 128 amino acids and having a molecular mass of 14.5kDa. GMCSF is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a sterile (0.2µm) filtered solution containing 10mM sodium phosphate, pH 7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50, as determined by TF-1 cell proliferation is 4.52ng/ml corresponding to a specific activity which is 2.2 x 10^5 units/mg.
More Info
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Introduction
GMCSF is a cytokine that controls the production, differentiation, and function of granulocytes and macrophages. The active form of GMCSF is found extracellularly as a homodimer. GMCSF has been localized to a cluster of related genes at chromosome region 5q31, which is known to be associated with interstitial deletions in the 5q- syndrome and acute myelogenous leukemia. Other genes in the cluster include those encoding interleukins 4, 5, and 13.
GM-CSF stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes. -
Synonyms
CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, Molgramostin, Sargramostim.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized GMCSF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GMCSF should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized GMCSF in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MAPTRPPSPV TRPWQHVDAI KEALSLLNNS NDTAAVMNET VDVVCEMFDP QEPTCVQTRL NLYKQGLRGS LTRLKSPLTL LAKHYEQHCP LTEETSCETQ SITFKSFKDS LNKFLFTIPF DCWGPVKK.
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Background
What is the molecular weight/Mw of GM-CSF PORCINE Protein?
GM-CSF PORCINE Protein has a total Mw of 14.5kDa.
What is the source or expression system of GM-CSF PORCINE Protein?
Escherichia Coli.
What is the Purity of GM-CSF PORCINE Protein?
GM-CSF PORCINE Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of GM-CSF PORCINE Protein?
The ED50, as determined by TF-1 cell proliferation is 4.52ng/ml corresponding to a specific activity which is 2.2 x 10^5 units/mg.
What is the amino acid sequence of GM-CSF PORCINE Protein?
MAPTRPPSPV TRPWQHVDAI KEALSLLNNS NDTAAVMNET VDVVCEMFDP QEPTCVQTRL NLYKQGLRGS LTRLKSPLTL LAKHYEQHCP LTEETSCETQ SITFKSFKDS LNKFLFTIPF DCWGPVKK.
What applications can GM-CSF PORCINE Protein be used in?
GM-CSF PORCINE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for GM-CSF PORCINE Protein?
The endotoxin level is minimal, GM-CSF PORCINE Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
NOV Human (260-357)Description:
Nephroblastoma Overexpressed (260-357 a.a.) Human Recombinant
Igfbp9, igfbp-9.
Product # :
CYT-1234Price :
Quantity :
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Shipped at Room temp
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Description
The IGFBP9 Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The IGFBP9 His-Tagged Fusion Protein, produced in E. coli, is a 18kDa protein containing 98 amino acid residues of the IGFBP9 Human, 260-357 amino acids.
Source
Escherichia Coli.
Formulation
Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Synonyms
Igfbp9, igfbp-9.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized IGFBP9 at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.
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Background
Nephroblastoma Overexpressed (NOV) is a part of the CCN (CTGF/CYR61/NOV) family which takes an important part in tissue repair and cellular signaling, differentiation and growth. NOV takes part in angiogenesis, extracellular matrix remodeling and cellular adhesion. NOV is also involved in reducing tumorgenicity and proliferation of certain cancer cell lines. NOV interacts with numerous proteins and participates in both internal and external cell signaling. NOV is expressed in tumors, including Wilm’s tumor and most nephroblastomas and is also exerts proangiogenic activities.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
BLyS Human, PlantDescription:
BAFF (BLyS) Human Recombinant, Plant
BAFF, BLYS, CD257, TALL1, THANK, ZTNF4, TALL-1, TNFSF20, TNFSF13B, B-cell Activating Factor.
Product # :
CYT-054Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
BAFF human Recombinant produced in Nicotiana benthamiana plant is a single glycosilated polypeptide chain containing 151 amino acids fragment (134-285).BAFF (C830H1277N223O242S5) is fused to a 10-His-tag at the N-terminal having the total molecular mass of 18-20kDa and purified by standard chromatographic techniques.
Source
Nicotiana benthamiana plant
Formulation
Lyophilized from 1mg/ml solution in 20 mM PBS buffer pH 7 and 0.2 M NaCl.
Purity
Greater than 97.0% as determined by Analysis by SDS-PAGE.
Biological Activity
The activity is determined by dose-dependent stimulation of proliferation B cell from Human PBMC. Cell proliferation was measured by MTT method.
*activity results may vary with PBMC donors.
ED50 ? 50ng/mlMore Info
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Introduction
BAFF binds to tnfrsf13b/taci and tnfrsf17/bcma. Tnfsf13/april binds to the same 2 receptors, together, they form a 2 ligands -2 receptors pathway involved in the stimulation of b- and t-cell function and the regulation of humoral immunity.A third b-cell specific baff-receptor (baffr/br3) promotes the survival of mature b-cells and the b-cell response.
B Lymphocyte Stimulator functions as a potent B-cell growth factor in costimulation assays.
Administration of BAFF Human recombinant to mice disrupts splenic B-cell and T-cell zones and results in elevated levels of serum immunoglobulin. -
Synonyms
BAFF, BLYS, CD257, TALL1, THANK, ZTNF4, TALL-1, TNFSF20, TNFSF13B, B-cell Activating Factor.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized BAFF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BAFF should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized BAFF in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
HHHHHHHHHH AVQGPEETVT QDCLQLIADS ETPTIQKGSY TFVPWLLSFK RGSALEEKEN KILVKETGYF FIYGQVLYTD KTYAMGHLIQ RKKVHVFGDE LSLVTLFRCI QNMPETLPNN SCYSAGIAKL EEGDELQLAI PRENAQISLD GDVTFFGALK LL
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Background
What is the molecular weight/Mw of BLYS Protein?
BLYS Protein has a total Mw of 19kDa.
What is the source or expression system of BLYS Protein?
Escherichia Coli.
What is the Purity of BLYS Protein?
BLYS Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of BLYS Protein?
The activity is determined by dose-dependent stimulation of proliferation B cell from Human PBMC. Cell proliferation was measured by MTT method.
What is the amino acid sequence of BLYS Protein?
HHHHHHHHHH AVQGPEETVT QDCLQLIADS ETPTIQKGSY TFVPWLLSFK RGSALEEKEN KILVKETGYF FIYGQVLYTD KTYAMGHLIQ RKKVHVFGDE LSLVTLFRCI QNMPETLPNN SCYSAGIAKL EEGDELQLAI PRENAQISLD GDVTFFGALK LL
What applications can BLYS Protein be used in?
BLYS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BLYS Protein?
The endotoxin level is minimal, BLYS Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
EGF Long HumanDescription:
Epidermal Growth Factor Long Human Recombinant
Urogastrone, URG, EGF.
Product # :
CYT-798Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Recombinant Human EGF Long produced in E.coli cells is a single non-glycosylated, polypeptide chain containing 106 amino acids and having a molecular mass of 12.3kDa. The EGF Long is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The EGF Long was lyophilized from a 0.2µm filtered concentrated solution in 10mM HCl.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by a cell proliferation assay using murine Balb/c 3T3 cells is less than 1.0 ng/ml, corresponding to a specific activity of > 1.0 × 106 IU/mg.More Info
-
Introduction
Epidermal growth factor has a profound effect on the differentiation of specific cells in vivo and is a potent mitogenic factor for a variety of cultured cells of both ectodermal and mesodermal origin. The EGF precursor is believed to exist as a membrane-bound molecule which is proteolytically cleaved to generate the 53-amino acid peptide hormone that stimulates cells to divide. EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture. Long EGF is a recombinant analog of Human EGF developed as a replacement for use in therapeutic cell culture applications as a like-for-like supplement for Recombinant Human or native EGF. It includes the Human EGF amino acid sequence plus a 53 amino acid N-terminal extension peptide.
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Synonyms
Urogastrone, URG, EGF.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized EGF Long although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EGF Long should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized EGF Long in sterile 100mM AcOH (acetic Acid) not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MFPAMPLSSL FANAVLRAQH LHQLAADTYK EFERAYIPEG QRYSIQVNFA HYGNSDSECP LSHDGYCLHD GVCMYIEALD KYACNCVVGY IGERCQYRDL KWWELR
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Background
What is the molecular weight/Mw of EGF Protein?
EGF Protein has a total Mw of 12.3kDa.
What is the source or expression system of EGF Protein?
Escherichia Coli.
What is the Purity of EGF Protein?
EGF Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of EGF Protein?
The ED50 as determined by a cell proliferation assay using murine Balb/c 3T3 cells is less than 1.0 ng/ml, corresponding to a specific activity of > 1.0 × 106 IU/mg.
What is the amino acid sequence of EGF Protein?
MFPAMPLSSL FANAVLRAQH LHQLAADTYK EFERAYIPEG QRYSIQVNFA HYGNSDSECP LSHDGYCLHD GVCMYIEALD KYACNCVVGY IGERCQYRDL KWWELR
What applications can EGF Protein be used in?
EGF Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for EGF Protein?
The endotoxin level is minimal, EGF Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
MCSFR HumanDescription:
Colony Stimulating Factor 1 Receptor Human Recombinant
Macrophage colony-stimulating factor 1 receptor, CSF-1 receptor (EC:2.7.10.1), CSF-1-R, CSF-1R, M-CSF-R, Proto-oncogene c-Fms, CD115, CSF1R, FMS.
Product # :
CYT-1068Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- More Info
Description
MCSFR produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 737 amino acids (20-517a.a.) and having a molecular mass of 82.1kDa. (Molecular size on SDS-PAGE will appear at approximately 70-100kDa).MCSFR is expressed with a 239 amino acid hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
MCSFR protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Measured by its ability to inhibit M-CSF dependent proliferation of M-NFS-60 mouse myelogenous leukemia lymphoblast cells. The ED50 for this effect is less or equal to 100ng/ml in the presence of 10 ng/ml M-CSF.
More Info
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Introduction
MCSFR which is also familiar as CSF1R, is part of the type3 subfamily of receptor tyrosine kinases. MCSFR is expressed mainly on cells of the monocyte and macrophage lineage, stem cells, and in the growing placenta. Most of the biological effects of this cytokine are mediated by MCSFR. MCSFR contains an extracellular ligand-binding domain, a single membrane-spanning segment, and an intracellular tyrosine kinase domain. Originally CSF1 and this receptor were implicated as vital for normal trophoblastic implantation as well as monocyte development. The role of CSF1/CSF1R in normal mammary gland development is actually very interesting since this connection has also been discovered in the biology of breast cancer with the results of abnormal expression of CSF1 and its receptor. Likewise, in Alzheimer's disease and after brain injuries an increased level of CSF1R was found in the microglia, which causes the microglia to become more active.
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Synonyms
Macrophage colony-stimulating factor 1 receptor, CSF-1 receptor (EC:2.7.10.1), CSF-1-R, CSF-1R, M-CSF-R, Proto-oncogene c-Fms, CD115, CSF1R, FMS.
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Physical Appearance
Sterile filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
IPVIEPSVPE LVVKPGATVT LRCVGNGSVE WDGPPSPHWT LYSDGSSSIL STNNATFQNT GTYRCTEPGD PLGGSAAIHL YVKDPARPWN VLAQEVVVFE DQDALLPCLL TDPVLEAGVS LVRVRGRPLM RHTNYSFSPW HGFTIHRAKF IQSQDYQCSA LMGGRKVMSI SIRLKVQKVI PGPPALTLVP AELVRIRGEA AQIVCSASSV DVNFDVFLQH NNTKLAIPQQ SDFHNNRYQK VLTLNLDQVD FQHAGNYSCV ASNVQGKHST SMFFRVVESA YLNLSSEQNL IQEVTVGEGL NLKVMVEAYP GLQGFNWTYL GPFSDHQPEP KLANATTKDT YRHTFTLSLP RLKPSEAGRY SFLARNPGGW RALTFELTLR YPPEVSVIWT FINGSGTLLC AASGYPQPNV TWLQCSGHTD RCDEAQVLQV WDDPYPEVLS QEPFHKVTVQ SLLTVETLEH NQTYECRAHN SVGSGSWAFI PISAGAHTHP PDEFLFTPLE PKSCDKTHTC PPCPAPELLG GPSVFLFPPK PKDTLMISRT PEVTCVVVDV SHEDPEVKFN WYVDGVEVHN AKTKPREEQY NSTYRVVSVL TVLHQDWLNG KEYKCKVSNK ALPAPIEKTI SKAKGQPREP QVYTLPPSRD ELTKNQVSLT CLVKGFYPSD IAVEWESNGQ PENNYKTTPP VLDSDGSFFL YSKLTVDKSR WQQGNVFSCS VMHEALHNHY TQKSLSLSPG KHHHHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
ThymalinDescription:
Thymulin
Product # :
HOR-047Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Thymulin Synthetic is a single, non-glycosylated polypeptide chain containing 9 amino acids, having a molecular mass of 858 Dalton and a Molecular formula of C33H54N12O15.
Formulation
The protein was lyophilized with no additives.
Purity
Greater than 97.0% as determined by analysis by RP-HPLC.
More Info
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Thymulin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Thymulin should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Thymulin in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
Pyr-Ala-Lys-Ser-Gln-Gly-Gly-Ser-Asn-OH.
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Background
Thymulin, a nonapeptide hormone, is produced primarily by the thymus gland and has been recognized for its pivotal role in the immune system. It plays a significant role in the maturation and differentiation of T lymphocytes, which are crucial for immune function. Beyond its immune-related functions, research has increasingly unveiled the diverse physiological roles of thymulin. This study aims to comprehensively investigate thymulin, shedding light on its immunological functions and exploring its potential applications in various aspects of health and medicine.
The primary objective of this research is to elucidate the mechanisms underlying thymulin's role in immune regulation. In vitro and in vivo experiments will be conducted to explore thymulin's interactions with immune cells, its impact on T cell development and function, and its potential modulation of immune responses. Understanding these mechanisms is fundamental for harnessing thymulin's immunomodulatory properties.
The second objective is to assess the clinical relevance of thymulin in immune-related disorders. Clinical trials and studies involving individuals with autoimmune diseases, immunodeficiencies, and age-related immune decline will be conducted to evaluate the potential therapeutic applications of thymulin. These investigations may offer insights into the use of thymulin as an immunomodulatory agent in various clinical settings.
The third objective is to explore the broader implications of thymulin in health and medicine. Research will investigate its potential roles in areas beyond immunology, such as neuroprotection, wound healing, and tissue regeneration. Understanding the multifaceted properties of thymulin may open new avenues for therapeutic interventions in various medical specialties.
By delving into the diverse functions of thymulin, this research aims to expand our knowledge of its physiological roles and clinical applications. The findings may have implications for the development of innovative approaches in immunology and healthcare, ultimately benefiting patients affected by immune-related disorders and other medical conditions.
What is the molecular weight/Mw of THYMALIN Protein?
THYMALIN Protein has a total Mw of 0.85kDa.
What is the Purity of THYMALIN Protein?
THYMALIN Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of THYMALIN Protein?
The biological functionality of THYMALIN Protein will be determined in the future.
What is the amino acid sequence of THYMALIN Protein?
Pyr-Ala-Lys-Ser-Gln-Gly-Gly-Ser-Asn-OH.
What applications can THYMALIN Protein be used in?
THYMALIN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for THYMALIN Protein?
The endotoxin level is minimal, THYMALIN Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
CGB HumanDescription:
CGB Human Recombinant
CGB3, CGB5, CGB7, CGB8, hCGB, CG-beta, CGB.
Product # :
HOR-007Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CGB Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 168 amino acids (21-165 a.a.) and having a molecular mass of 17.9kDa. CGB is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CGB protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Glycoprotein hormones are heterodimers consisting of a common alpha subunit and a unique beta subunit which confers biological specificity. CGB is a member of the glycoprotein hormone beta chain family and is the beta 3 subunit of (CG). CG is produced by the trophoblastic cells of the placenta and stimulates the ovaries. The beta subunit of CG is encoded by 6 genes which are arranged in tandem and inverted pairs on chromosome 19q13.3 and contiguous with the luteinizing hormone beta subunit gene.
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Synonyms
CGB3, CGB5, CGB7, CGB8, hCGB, CG-beta, CGB.
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Physical Appearance
Sterile filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSSKEPLRP RCRPINATLA VEKEGCPVCI TVNTTICAGY CPTMTRVLQG VLPALPQVVC NYRDVRFESI RLPGCPRGVN PVVSYAVALS CQCALCRRST TDCGGPKDHP LTCDDPRFQD SSSSKAPPPS LPSPSRLPGP SDTPILPQ.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
RPS27A Human, BiotinDescription:
Ubiquitin Biotinylated Human Recombinant
Ubiquitin, Ribosomal Protein S27a, CEP80, UBA80, UBCEP1, UBCEP80, HUBCEP80, RPS27A.
Product # :
PRO-629Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Human RPS27A protein biotinylated with NHS-biotin produced in E.Coli is a single, non-glycosylated polypeptide chain containing a total of 76 amino acids and having a molecular mass of 8.6 kDa.
Source
Escherichia Coli.
Formulation
The RPS27A is supplied in 1x PBS and 0.05% PBS.
Purity
RPS27A Protein biotinilation is determined by Western Blotting and ELISA analysis using streptavidin–HRP conjugated as a detection reagent. Free biotin is eliminated by dialysis against PBS. Protein concentration is determined by 280nm absorbance.
More Info
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Introduction
Recombinant Human Ubiquitin having the accession number of P62988 was conjugated to Biotin. RPS27A is a small protein composed of 76 amino acids. RPS27A is found only in eukaryotic organisms among which shows strong sequence conservation. The RPS27A protein is present in all cell types, thus giving rise to its name.
RPS27A is found either in free form or conjugated to proteins through a covalent bond between the glycine at the C-terminal end and the side chains of lysine.
The connection of multiple copies of RPS27A targets the proteins for degradation by the 26S proteosome. RPS27A ligation is an ATP-dependent multi-step process. RPS27A is activated by the E1 enzyme. The attachment of RPS27A to the target protein is catalyzed by the E2 enzyme acting in concert with E3 which is involved in the recognition of the substrate protein. -
Synonyms
Ubiquitin, Ribosomal Protein S27a, CEP80, UBA80, UBCEP1, UBCEP80, HUBCEP80, RPS27A.
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Physical Appearance
Sterile Filtered colorless liquid formulation.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
CCN1 HumanDescription:
Cysteine-Rich Angiogenic Inducer 61 Human Recombinant
CYR61, Protein CYR61, Cysteine-rich angiogenic inducer 61, IGF-binding protein 10, IGFBP-10, IBP-10, Protein GIG1, CCN family member 1, CCN1, GIG1, IGFBP10.
Product # :
CYT-164Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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- source
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Description
CYR61 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 357 amino acids and having a molecular mass of 39.5kDa.The CYR61 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2m filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50 was determined by the proliferation of mouse 3T3 cells is < 2.0 ug/ml, corresponding to a specific activity of > 500 units/mg.More Info
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Introduction
CYR61 is a growth factor-inducible, immediate-early gene that has multifaceted activities in various cancers. CYR61 is a secreted, cysteine-rich, binding protein which is encoded by a growth factor-inducible immediate-early gene. Acting as an extracellular, matrix-associated signaling molecule, CYR61 promotes the adhesion of endothelial cells through interaction with integrin and enhances growth factor-induced DNA synthesis in the same cell type.
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Synonyms
CYR61, Protein CYR61, Cysteine-rich angiogenic inducer 61, IGF-binding protein 10, IGFBP-10, IBP-10, Protein GIG1, CCN family member 1, CCN1, GIG1, IGFBP10.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized CYR61 Human although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CYR61 should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized CYR61 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
TCPAACHCPL EAPKCAPGVG LVRDGCGCCK VCAKQLNEDC SKTQPCDHTK GLECNFGASS TALKGICRAQ SEGRPCEYNS RIYQNGESFQ PNCKHQCTCI DGAVGCIPLC PQELSLPNLG CPNPRLVKVT GQCCEEWVCD EDSIKDPMED QDGLLGKELG FDASEVELTR NNELIAVGKG SSLKRLPVFG MEPRILYNPL QGQKCIVQTT SWSQCSKTCG TGISTRVTND NPECRLVKET RICEVRPCGQ PVYSSLKKGK KCSKTKKSPE PVRFTYAGCL SVKKYRPKYC GSCVDGRCCT
PQLTRTVKMR FRCEDGETFS KNVMMIQSCK CNYNCPHANE AAFPFYRLFN DIHKFRD -
Background
Title: Cysteine-Rich Angiogenic Inducer 61 Human Recombinant: A Potential Regulator of Angiogenesis
Abstract:
Cysteine-rich angiogenic inducer 61 (CYR61) is an important extracellular matrix-associated protein that plays a significant role in angiogenesis and cell adhesion. This research paper provides a comprehensive analysis of human recombinant CYR61, focusing on its production, characterization, and potential applications in regulating angiogenesis. The paper discusses the significance of CYR61 in physiological and pathological angiogenesis, including wound healing, tumor development, and cardiovascular diseases. Furthermore, it explores ongoing research and clinical trials investigating the therapeutic potential of recombinant CYR61 in various pathological conditions. The information presented in this paper aims to enhance our understanding of human recombinant CYR61 and its utility as a research tool and a potential regulator of angiogenesis.Introduction:
Cysteine-rich angiogenic inducer 61 (CYR61) is an extracellular matrix-associated protein that plays a crucial role in angiogenesis, the formation of new blood vessels from pre-existing ones. Human recombinant CYR61, produced through genetic engineering techniques, provides researchers with a valuable tool to study its biological functions and explore its therapeutic potential.Production and Characterization:
Recombinant CYR61 is typically generated using expression systems such as mammalian cells or bacteria. The protein is then purified and characterized to ensure its structural integrity and functional activity. Quality control measures are implemented to confirm the specificity and bioactivity of the recombinant CYR61.Role in Angiogenesis:
CYR61 is involved in various aspects of angiogenesis, including endothelial cell proliferation, migration, and tube formation. It interacts with integrins and other cell surface receptors to modulate signaling pathways involved in angiogenic processes. Recombinant CYR61 serves as a valuable tool for studying the mechanisms underlying angiogenesis and exploring its potential as a therapeutic target.Therapeutic Implications:
The dysregulation of angiogenesis is associated with several pathological conditions, including cancer, cardiovascular diseases, and chronic wounds. Recombinant CYR61 has shown promise as a potential regulator of angiogenesis and a therapeutic agent. It can be used to promote or inhibit angiogenesis, depending on the specific context. Ongoing research and clinical trials are investigating the therapeutic applications of recombinant CYR61 in various diseases, including cancer and ischemic disorders.Conclusion:
Human recombinant CYR61 is a valuable research tool and a potential regulator of angiogenesis. Its production, characterization, and applications in modulating angiogenic processes contribute to our understanding of angiogenesis and the development of novel therapeutic interventions. Continued research and clinical trials exploring the therapeutic potential of recombinant CYR61 offer promising prospects for improving outcomes in cancer, cardiovascular diseases, and wound healing.What is the molecular weight/Mw of CCN1 Protein?
CCN1 Protein has a total Mw of 39.5kDa.
What is the source or expression system of CCN1 Protein?
Escherichia Coli.
What is the Purity of CCN1 Protein?
CCN1 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CCN1 Protein?
The ED50 was determined by the proliferation of mouse 3T3 cells is < 2.0 ug/ml, corresponding to a specific activity of > 500 units/mg.
What is the amino acid sequence of CCN1 Protein?
TCPAACHCPL EAPKCAPGVG LVRDGCGCCK VCAKQLNEDC SKTQPCDHTK GLECNFGASS TALKGICRAQ SEGRPCEYNS RIYQNGESFQ PNCKHQCTCI DGAVGCIPLC PQELSLPNLG CPNPRLVKVT GQCCEEWVCD EDSIKDPMED QDGLLGKELG FDASEVELTR NNELIAVGKG SSLKRLPVFG MEPRILYNPL QGQKCIVQTT SWSQCSKTCG TGISTRVTND NPECRLVKET RICEVRPCGQ PVYSSLKKGK KCSKTKKSPE PVRFTYAGCL SVKKYRPKYC GSCVDGRCCT
PQLTRTVKMR FRCEDGETFS KNVMMIQSCK CNYNCPHANE AAFPFYRLFN DIHKFRD
What applications can CCN1 Protein be used in?
CCN1 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CCN1 Protein?
The endotoxin level is minimal, CCN1 Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Y.Enterocolitica (O:9) YopEDescription:
Yersinia Enterocolitica (O:9) YopE Recombinant
Outer membrane virulence protein YopE, yopE, yop25.
Product # :
PRO-2576Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
- source
- formulation
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Description
Recombinant Yersinia Enterocolitica (O:9) YopE in E.coli is a non-glycosylated, polypeptide chain having a calculated molecular mass of 24kDa. Y.Enterocolitica (O:9) YopE is expressed with a -10x His tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Y.Enterocolitica (O:9) YopE is supplied in 20mM HEPES buffer pH-7.6, 250mM NaCl and 20% glycerol.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
A main factor of pathogenic Yersinia enterocolitica strains is a plasmid-encoded type 3 secretion system, through which Yersinia outer proteins (Yops) are injected into the host cell. Yop E is a GTPase activation protein which controls pore formation by activating small Rho GTPase, causing inhibition of actin polymerization.
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Synonyms
Outer membrane virulence protein YopE, yopE, yop25.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
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Immunological Activity
Binds IgG- and IgM-type human antibodies.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Activin-A RatDescription:
Activin-A Rat Recombinant
Inhba, Inhibin beta A, FSH releasing protein.
Product # :
CYT-147Price :
Quantity :
Shipping Method :
Shipped at Room temp
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- description
- source
- formulation
- purity
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Description
Active form Activin-A Rat Recombinant produced in e.coli is a homodimeric, non-glycosylated, polypeptide chain containing 2 x 117 amino acids and having a molecular weight of 26.2kDa.The Active form Activin-A is purified by standard chromatographic techniques.
Source
E.Coli.
Formulation
Rat Activin-A was lyophilized from a concentrated 1mg/ml protein solution containing 0.02% TFA.
Purity
Greater than 95% as obsereved by SDS-PAGE.
Biological Activity
Biological activity is assessed by the ability to induce cytoxicity of MPC-11 cells and was found to be 8.8ng/mlMore Info
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Introduction
Activins are homodimers or heterodimers of the different β subunit isoforms, part of the TGFβ family. Mature Activin A has two 116 amino acids residues βA subunits (βA-βA). Activin displays an extensive variety of biological activities, including mesoderm induction, neural cell differentiation, bone remodelling, haematopoiesis, and reproductive physiology. Activins takes part in the production and regulation of hormones such as FSH, LH, GnRH and ACTH. Cells that are identified to express Activin A include fibroblasts, endothelial cells, hepatocytes, vascular smooth muscle cells, macrophages, keratinocytes, osteoclasts, bone marrow monocytes, prostatic epithelium, neurons, chondrocytes, osteoblasts, Leydig cells, Sertoli cells, and ovarian granulosa cells.
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Synonyms
Inhba, Inhibin beta A, FSH releasing protein.
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Physical Appearance
Lyophilized freeze dried powder.
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Stability
Lyophilized Activin-A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Activin-A should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
Rat INHBA protein should be reconstituted in distilled pyrogen free water to a concentration of 100ug /ml which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MGLECDGKVN ICCKKQFFVS FKDIGWNDWI IAPSGYHANY CEGECPSHIA GTSGSSLSFH STVINHYRMR GHSPFANLKS CCVPTKLRPM SMLYYDDGQN IIKKDIQNMI VEECGCS.
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Background
What is the molecular weight / Mw of Activin A Protein?
Activin A Protein has a total Mw of 26.2 kDa.
What is the source or expression system of Activin A Protein?
Ecoli
What is the Purity of Activin A Protein?
Activin A Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of Activin A Protein?
Biological activity is assessed by the ability to induce cytoxicity of MPC-11 cells and was found to be 8.8ng/ml corresponding to a specific activity of 110,000units/mg.
What is the endotoxin level for Activin A Protein?
The endotoxin level is minimal, ACTIVIN A Protein was purified using conventional chromatography techniques.
What is the amino acid sequence of ACTIVIN A Protein?
MGLECDGKVN ICCKKQFFVS FKDIGWNDWI IAPSGYHANY CEGECPSHIA GTSGSSLSFH STVINHYRMR GHSPFANLKS CCVPTKLRPM SMLYYDDGQN IIKKDIQNMI VEECGCS.
What applications can ACTIVIN A Protein be used in?
ACTIVIN A Protein can probably be used in western blot, ELISA and Lateral Flow.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Cyclophilin A RatDescription:
Cyclophilin-A Rat Recombinant
Peptidyl-prolyl cis-trans isomerase A, EC:5.2.1.8, PPIase A, Cyclophilin A, Cyclosporin A-binding protein, Rotamase A, p1B15, p31, Ppia.
Product # :
ENZ-938Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
Cyclophilin-A Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (Val2-Leu164) containing 173 amino acids including a 10 aa His tag at N-terminus. The total calculated molecular mass is 19kDa.
Source
Escherichia Coli.
Formulation
Cyclophilin-A was filtered (0.4µm) and lyophilized from 0.5mg/ml solution in phosphate buffered saline and 5%(w/v) trehalose.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and accelerate the folding of proteins. Cyclophilin-A is a cyclosporin binding-protein and may play a role in cyclosporin A-mediated immunosuppression. Cyclophilin-A can also interact with several HIV proteins, including p55 gag, Vpr, and capsid protein, and has been shown to be necessary for the formation of infectious HIV virions. Multiple pseudogenes that map to different chromosomes have been reported.
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Synonyms
Peptidyl-prolyl cis-trans isomerase A, EC:5.2.1.8, PPIase A, Cyclophilin A, Cyclosporin A-binding protein, Rotamase A, p1B15, p31, Ppia.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Cyclophilin-A is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
MKHHHHHHASVNPTVFFDIT ADGEPLGRVC FELFADKVPK TAENFRALST GEKGFGYKGS SFHRIIPGFM CQGGDFTRHN GTGGKSIYGE KFEDENFILK HTGPGILSMA NAGPNTNGSQ FFICTAKTEW LDGKHVVFGK VKEGMSIVEA MERFGSRNGK TSKKITISDC GQL.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
MSMB HumanDescription:
Beta-Microseminoprotein Human Recombinant
Beta-microseminoprotein, Prostate secreted seminal plasma protein, Prostate secretory protein PSP94, Seminal plasma beta-inhibin, Immunoglobulin-binding factor, MSP, PSP, PSP57, PSP94, PSP-94, MSP-beta, beta-MSP, Microseminoprotein, IGBF, PN44, MSMB, MSP-B, MSPB, PRPS, Prostatic Secretory Protein.
Product # :
PRO-598Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
MSMB Recombinant Human produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 104 amino acids and having a molecular mass of 12 kDa. The MSMB is fused to His tag at N-Terminus.The Human MSMB is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The sterile filtered concentrated (0.5mg/ml) protein solution was lyophilized with 20mM Tris & 20mM NaCl pH-7.5.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Microseminoprotein is a member of the immunoglobulin binding factor family. It is synthesized by the epithelial cells of the prostate gland and secreted into the seminal plasma. This protein has inhibin-like activity. It may have a role as an autocrine paracrine factor in uterine, breast and other female reproductive tissues. The expression of the encoded protein is found to be decreased in prostate cancer. Two alternatively spliced transcript variants encoding different isoforms are described for this gene. The use of alternate polyadenylation sites has been found for this gene.
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Synonyms
Beta-microseminoprotein, Prostate secreted seminal plasma protein, Prostate secretory protein PSP94, Seminal plasma beta-inhibin, Immunoglobulin-binding factor, MSP, PSP, PSP57, PSP94, PSP-94, MSP-beta, beta-MSP, Microseminoprotein, IGBF, PN44, MSMB, MSP-B, MSPB, PRPS, Prostatic Secretory Protein.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time.
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Solubility
Add deionized water to a working concentration of 0.5mg/ml and let the lyophilized pellet dissolve completely.
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Amino Acid Sequence
MKHHHHHHAS SCYFIPNEGV PGDSTRKCMD LKGNKHPINS EWQTDNCETC TCYETEISCC TLVSTPVGYD KDNCQRIFKK EDCKYIVVEK KDPKKTCSVSEWII.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
SDCBP2 HumanDescription:
Syndecan Binding Protein 2 Human Recombinant
SITAC, SITAC18, ST-2, Syntenin-2, Syndecan-binding protein 2.
Product # :
PRO-1297Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
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Description
SDCBP2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 315 amino acids (1-292 a.a.) and having a molecular mass of 34.0kDa. SDCBP2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
SDCBP2 protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
SDCBP2 has two class II PDZ domains. PDZ domains assist protein-protein interactions by attaching to the cytoplasmic C-terminus of transmembrane proteins, and PDZ-containing proteins mediate cell signaling and the organization of protein complexes. SDCBP2 attaches to phosphatidylinositol 4, 5-bisphosphate (PIP2) and take part in nuclear PIP2 arrangement and cell division.
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Synonyms
SITAC, SITAC18, ST-2, Syntenin-2, Syndecan-binding protein 2.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMSSLYPS LEDLKVDQAI QAQVRASPKM PALPVQATAI SPPPVLYPNL AELENYMGLS LSSQEVQESL LQIPEGDSTA VSGPGPGQMV APVTGYSLGV RRAEIKPGVR EIHLCKDERG KTGLRLRKVD QGLFVQLVQA NTPASLVGLR FGDQLLQIDG RDCAGWSSHK AHQVVKKASG DKIVVVVRDR PFQRTVTMHK DSMGHVGFVI KKGKIVSLVK GSSAARNGLL TNHYVCEVDG QNVIGLKDKK IMEILATAGN VVTLTIIPSV IYEHMVKKLP PVLLHHTMDH SIPDA.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
HPCAL1 HumanDescription:
Hippocalcin-Like 1 Human Recombinant
Hippocalcin-Like 1, HLP2, BDR1, Calcium-Binding protein BDR-1, Visinin-Like protein 3, VILIP-3
Product # :
PRO-254Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
HPCAL1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 213amino acids (1-193a.a.) and having a molecular wieght of 24.4kDa. The HPCAL1 is fused to 20a.a. His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The HPCAL1 protein solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH8.0) containing 1mM DTT 0.2M NaCl and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
HPCAL1, participates in neuron-specific calcium-binding proteins family found in the retina and brain. HPCAL1 is extremely comparable to human hippocalcin protein and almost equal to the rat and mouse hippocalcin like-1 proteins. HPCAL1 takes part in the calcium-dependent regulation of rhodopsin phosphorylation and can have importance in neuronal signalling in the central nervous system.
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Synonyms
Hippocalcin-Like 1, HLP2, BDR1, Calcium-Binding protein BDR-1, Visinin-Like protein 3,
VILIP-3 -
Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGKQNSKLRP EVLQDLRENT EFTDHELQEW YKGFLKDCPT GHLTVDEFKK IYANFFPYGD ASKFAEHVFR TFDTNGDGTI DFREFIIALS VTSRGKLEQK LKWAFSMYDL DGNGYISRSE MLEIVQAIYK MVSSVMKMPE DESTPEKRTD KIFRQMDTNN DGKLSLEEFI RGAKSDPSIV RLLQCDPSSA SQF
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.