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1000 results found for “influenza”
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Name :
CXCL8 Human (1-72)Description:
Interleukin-8 (1-72 a.a.) Human Recombinant (CXCL8)
IL-8, CXCL8, Monocyte-derived neutrophil chemotactic factor, MDNCF, T-cell chemotactic factor, Neutrophil-activating protein 1, NAP-1, Protein 3-10C, Granulocyte chemotactic protein 1, GCP-1, Monocyte-derived neutrophil-activating peptide, MONAP, Emoctakin, K60, NAF, LECT, LUCT, 3-10C, LYNAP, SCYB8, TSG-1, AMCF-I, b-ENAP.
Product # :
CHM-231Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Interleukin-8 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 72 amino acids and having a molecular mass of 8452 Dalton. The IL-8 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The IL-8 was lyophilized from a concentrated (1mg/ml) solution in water containing no additives.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Specific Activity of IL8 in chemotaxis of donor PBL neutrophils, threshold concentration corresponding to 10-100 ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.sds-page
Citations
More Info
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Introduction
Interleukin-8 (IL-8) is a chemokine produced by macrophages and other cell types such as epithelial cells. It is also synthesized by endothelial cells, which store IL-8 in their storage vesicles, the Weibel-Palade bodies. When first encountering an antigen, the primary cells to encounter it are the macrophages who phagocytose the particle. Upon processing, they release chemokines to signal other immune cells to come in to the site of inflammation. IL-8 is one such chemokine. It serves as a chemical signal that attracts neutrophils at the site of inflammation, and therefore is also known as Neutrophil Chemotactic Factor.
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Synonyms
IL-8, CXCL8, Monocyte-derived neutrophil chemotactic factor, MDNCF, T-cell chemotactic factor, Neutrophil-activating protein 1, NAP-1, Protein 3-10C, Granulocyte chemotactic protein 1, GCP-1, Monocyte-derived neutrophil-activating peptide, MONAP, Emoctakin, K60, NAF, LECT, LUCT, 3-10C, LYNAP, SCYB8, TSG-1, AMCF-I, b-ENAP.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Interleukin-8 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL8 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 Interleukin-8 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
The sequence of the first five N-terminal amino acids was determined and was found to be Ser-Ala-Lys-Glu-Leu.
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Background
What is the molecular weight/Mw of CXCL8 HUMAN (1-72) Protein?
CXCL8 HUMAN (1-72) Protein has a total Mw of 8.45kDa.
What is the source or expression system of CXCL8 HUMAN (1-72) Protein?
Escherichia Coli.
What is the Purity of CXCL8 HUMAN (1-72) Protein?
CXCL8 HUMAN (1-72) Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL8 HUMAN (1-72) Protein?
Specific Activity of IL8 in chemotaxis of donor PBL neutrophils, threshold concentration corresponding to 10-100 ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.
What is the amino acid sequence of CXCL8 HUMAN (1-72) Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Ser-Ala-Lys-Glu-Leu.
What applications can CXCL8 HUMAN (1-72) Protein be used in?
CXCL8 HUMAN (1-72) Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL8 HUMAN (1-72) Protein?
The endotoxin level is minimal, CXCL8 HUMAN (1-72) Protein was purified using conventional chromatography techniques.
Who supplies recombinant CXCL8 HUMAN (1-72) that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.
Where can I order bulk mg quantities of CXCL8 HUMAN (1-72)?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
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 :
DsbG E.ColiDescription:
Thiol Disulfide Interchange Protein E.Coli Recombinant DsbG
Thiol:disulfide interchange protein dsbG, dsbG, ybdP, b0604, JW0597.
Product # :
HSP-024Price :
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Shipped with Ice Packs
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Description
Recombinant DsbG produced in E.Coli is a single, non-glycosylated polypeptide chain containing 232 amino acids and having a molecular mass of 25.8 kDa. DsbG is purified by conventional chromatography techniques.
Source
Escherichia Coli.
Formulation
The DsbG protein solution contains 20mM Tris-HCl, pH-8, 2mM EDTA and 10% Glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Dsb proteins are in charge for the formation and rearrangement of disulfide bonds during the folding of secreted and membrane proteins in bacteria. DsbG has disulfide bond isomerase and chaperone activity. DsbG interacts with refolding intermediates of chemically denatured citrate synthase and prevents their aggregation in vitro. DsbG shares sequnce homology with DsbC. DsbG forms a stable periplasmic dimer and displays an equilibrium constant with glutathione comparable with DsbA and DsbC. DsbG is expressed at roughly 25% level of DsbC.
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Synonyms
Thiol:disulfide interchange protein dsbG, dsbG, ybdP, b0604, JW0597.
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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
MEELPAPVKA IEKQGITIIK TFDAPGGMKG YLGKYQDMGV TIYLTPDGKH AISGYMYNEK GENLSNTLIE KEIYAPAGRE MWQRMEQSHW LLDGKKDAPV IVYVFADPFC PYCKQFWQQA RPWVDSGKVQ LRTLLVGVIK PESPATAAAI LASKDPAKTW QQYEASGGKL KLNVPANVST EQMKVLSDNE KLMDDLGANV TPAIYYMSKE NTLQQAVGLP DQKTLNIIMG NK.
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 29 Human, HisDescription:
Interleukin-29 Human Recombinant, His Tag
Interferon lambda-1, IL-29, IL29, IFN-lambda-1, Cytokine Zcyto21, Interleukin-29.
Product # :
CYT-864Price :
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Description
IL 29 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 206 amino acids (20-200 a.a) and having a molecular mass of 22.7kDa.IL 29 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
IL 29 protein solution (1mg/ml) containing 20mM Tris-HCl (pH8.0) and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
Citations
More Info
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Introduction
IL-29 is distantly related to type I interferons and the IL-10 family. Expression of IL-29 is induced by viral infection which interacts with a heterodimeric class II cytokine receptor that consists of interleukin 10 receptor, beta (IL10RB) and interleukin 28 receptor, alpha. IL-29 exhibits common features with type I IFNs such as antiviral activity, antiproliferative activity and in vivo antitumour activity.
IL-29 acts similarly to IFNs, but is less effective generally and has activity in a more limited range of cell lines. IFN-ambda 1, IFN-lambda 2 and IFN-lambda3 are closely positioned genes on human chromosome 19.
IL-29 induces ELR(-) CXC chemokine mRNA in human peripheral blood mononuclear cells, in an IFN-gamma-independent manner.
IL-29 is able to generate tolerogenic DCs, an activity that could thwart IFN-beta functions. IL-29 produced in response to viral infection, activates both monocytes and macrophages producing a restricted panel of cytokines and therefore is an important factor in activating innate immune responses at the site of viral infection.
IFN-Lambda 1 antiviral and antiproliferative activity requires Interferon-Lambda 2 receptor tyrosine residues. -
Synonyms
Interferon lambda-1, IL-29, IL29, IFN-lambda-1, Cytokine Zcyto21, Interleukin-29.
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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
MGSSHHHHHH SSGLVPRGSH MGSHMGPVPT SKPTTTGKGC HIGRFKSLSP QELASFKKAR DALEESLKLK NWSCSSPVFP GNWDLRLLQV RERPVALEAE LALTLKVLEA AAGPALEDVL DQPLHTLHHI LSQLQACIQP QPTAGPRPRG RLHHWLHRLQ EAPKKESAGC LEASVTFNLF RLLTRDLKYV ADGNLCLRTS THPEST.
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 :
CFP Human, NativeDescription:
Complement Factor Properdin Human
Properdin, Complement factor P, CFP, PFC, Complement factor properdin, BFD, PFD, Properdin.
Product # :
PRO-2702Price :
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Description
CFP Human produced in Human plasma having a molecular weight of 53kDa.
Source
Human Plasma.
Formulation
CFP solution contains PBS, pH 7.2.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Complement Factor Properdin (CFP) which is a plasma glycoprotein, is a positive regulator of the alternative complement pathway of the innate immune system. CFP binds and stabilizes the C3- and C5-convertase enzyme complexes in a feedback loop that eventually ends with formation of the membrane attack complex and lysis of the target cell. Mutations in CFP lead to 2 forms of properdin deficiency that cause high susceptibility to meningococcal infections.
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Synonyms
Properdin, Complement factor P, CFP, PFC, Complement factor properdin, BFD, PFD, Properdin.
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Physical Appearance
Sterile filtered solution.
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Stability
CFP Human is stable at 4°C if entire vial will be used within 2-4 weeks.Store, frozen below -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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Human Virus Test
Plasma from each donor has been tested and found negative for antibody to HIV-1, HIV-2, HCV, HTLV-I &II, STS and HBSAG.
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 :
Treponema p17 16.4kDaDescription:
Treponema pallidum p17, 16.4kDa Recombinant
Product # :
TRP-252Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Recombinant Treponema p17 produced in E.coli is a non-glycosylated polypeptide chain having a molecular mass of 16.4kDa and fused to a His tag at N-terminus.
Source
Escherichia Coli.
Formulation
Lyophilized from 1mg/ml in 20mM sodium carbonate pH-10.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Treponema pallidum is a gram-negative spirochaete bacterium and is considered to be metabolically crippled. There are at least four known subspecies: T. pallidum pallidum, T. pallidum pertenue, T. pallidum carateum and T. pallidum endemicum. The helical structure of T. pallidum pallidum allows it to move in a corkscrew motion through viscous mediums such as mucus. Treponema pallidum sub sp. pallidum has one of the smallest bacterial genomes at 1.14 million base pairs (Mb) and has limited metabolic capabilities, reflecting its adaptation through genome reduction to the rich environment of mammalian tissue.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Treponema p17 although stable at room temperature for 4 weeks, should be stored below -18°C. Please prevent freeze thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Treponema p17 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 :
Adipsin Human, Sf9Description:
Complement Factor D Human Recombinant, Sf9
Complement Factor D (Adipsin), Properdin Factor D, D Component Of Complement (Adipsin), C3 Convertase Activator, EC 3.4.21.46, ADIPSIN, PFD, AND, DF, Complement Factor D Preproprotein, Complement Factor D, EC 3.4.21, Complement factor D.
Product # :
PRO-2213Price :
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Description
Adipsin produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 241 amino acids (21-253a.a.) and having a molecular mass of 26.01kDa. (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). Adipsin is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
Adipsin protein solution (1mg/ml) contains phosphate buffered saline (pH7.4).
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Complement Factor D (Adipsin), which belongs to the trypsin family of peptidases, is involved in the alternative complement pathway of the complement system where it cleaves factor B. In the alternative complement pathway, Adipsin is best known for its role in humoral suppression of infectious agents. In addition, Adipsin is a serine protease which is secreted by adipocytes into the bloodstream. Ultimately, Adipsin has a high level of expression in fat, proposing a role for adipose tissue in immune system biology.
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Synonyms
Complement Factor D (Adipsin), Properdin Factor D, D Component Of Complement (Adipsin), C3 Convertase Activator, EC 3.4.21.46, ADIPSIN, PFD, AND, DF, Complement Factor D Preproprotein, Complement Factor D, EC 3.4.21, Complement factor D.
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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
PPRGRILGGR EAEAHARPYM ASVQLNGAHL CGGVLVAEQW VLSAAHCLED AADGKVQVLL GAHSLSQPEP SKRLYDVLRA VPHPDSQPDT IDHDLLLLQL SEKATLGPAV RPLPWQRVDR DVAPGTLCDV AGWGIVNHAG RRPDSLQHVL LPVLDRATCN RRTHHDGAIT ERLMCAESNR RDSCKGDSGG PLVCGGVLEG VVTSGSRVCG NRKKPGIYTR VASYAAWIDS VLAVEHHHHH H.
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 :
Borrelia NapADescription:
Borrelia Burgdorferi Neutrophil Activating Protein A Recombinant
Product # :
BOR-014Price :
Quantity :
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Description
Recombinant Borrelia Burgdorferi NapA produced in E.coli is a non-glycosylated, full-length polypeptide chain having a calculated molecular mass of 21 kDa. Borrelia NapA is expressed with a -6x His tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Borrelia NapA is supplied in 16mM HEPES buffer pH-7.8, 400mM NaCl and 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Borrelia belongs to a genus of bacteria of the spirochete phylum. Borrelia causes borreliosis, which is a zoonotic, vector-borne disease transmitted mainly by ticks and some by lice, depending on the species. Of the 36 known species of Borrelia, 12 are distinguished to cause Lyme disease or borreliosis and are transmitted by ticks. The main Borrelia species causing Lyme disease are Borrelia burgdorferi, Borrelia afzelii, and Borrelia garinii. The Borrelia genus members have a linear chromosome which is about 900 kbp in length as well as an excess of both linear and circular plasmids in the 5-220 kbp size range. The plasmids are atypical, as compared to most bacterial plasmids, since they contain many paralogous sequences, a large number of pseudogenes and, in some cases, essential genes. Moreover, a number of the plasmids have features suggesting that they are prophages.
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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.
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 :
FHL3 HumanDescription:
Four And A Half LIM Domains 3 Human Recombinant
Four And A Half LIM Domains 3, SLIM2, Skeletal Muscle LIM-Protein 2, FHL-3, SLIM-2, Four And A Half LIM Domains Protein 3, LIM-Only Protein FHL3.
Product # :
PRO-1757Price :
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Shipping Method :
Shipped with Ice Packs
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Description
FHL3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 303 amino acids (1-280 a.a) and having a molecular mass of 33.6kDa. FHL3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
FHL3 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Four and a half LIM domains 3 (FHL3) belongs to a family of proteins containing a four-and-a-half LIM domain, which is a highly conserved double zinc finger motif. FHL3 has been shown to interact with the cancer developmental regulators SMAD2, SMAD3, and SMAD4, the skeletal muscle myogenesis protein MyoD, and the high-affinity IgE beta chain regulator MZF-1. FHL3 is involved in tumor suppression, repression of MyoD expression, and repression of IgE receptor expression. Two transcript variants encoding different isoforms have been found for this gene.
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Synonyms
Four And A Half LIM Domains 3, SLIM2, Skeletal Muscle LIM-Protein 2, FHL-3, SLIM-2, Four And A Half LIM Domains Protein 3, LIM-Only Protein FHL3.
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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).Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMSESFDC AKCNESLYGR KYIQTDSGPY CVPCYDNTFA NTCAECQQLI GHDSRELFYE DRHFHEGCFR CCRCQRSLAD EPFTCQDSEL LCNDCYCSAF SSQCSACGET VMPGSRKLEY GGQTWHEHCF LCSGCEQPLG SRSFVPDKGA HYCVPCYENK FAPRCARCSK TLTQGGVTYR DQPWHRECLV CTGCQTPLAG QQFTSRDEDP YCVACFGELF APKCSSCKRP IVGLGGGKYV SFEDRHWHHN CFSCARCSTS LVGQGFVPDG DQVLCQGCSQ AGP.
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 :
SIV p55Description:
Simian Immunodeficiency Virus p55 Recombinant
Product # :
SIV-114Price :
Quantity :
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Shipped with Ice Packs
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Description
Recombinant SIV p55- Strains: SIV mac 23g and SIV smH4 is glycosylated with N-linked sugars and produced using baculovirus vectors in insect cells.
Source
Baculovirus Insect Cells.
Formulation
SIV p55 Protein solution containing 10mM Tris, pH 8, 140mM NaCl & 400mM L-Arginine.
Purity
Greater than 90.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Citations
More Info
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Introduction
Simian immunodeficiency virus, SIV, is a retrovirusthat is found in strains, having the HIV-1and HIV-2specific strains that infect humans. SIV strains may cause an AIDS-like immune deficiency known as SAIDS (simian acquired immunodeficiency syndrome) if they cross species boundaries. HIV-2 is more similar to SIV strains than to HIV-1, suggesting for the first time the simian origin of HIV. HIV-2 is derived from the SIV strain found in sooty mangabeys whereas HIV-1, the predominant virus found in humans, is derived from SIV strains infecting chimpanzees.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Recombinant SIV p55 although stable at 4°C for 3 weeks, should be stored below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA). Please avoid 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.
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Name :
MIF Human, GSTDescription:
Macrophage Migration Inhibitor Factor Human Recombinant, GST tag
Macrophage Migration Inhibitory Factor (Glycosylation-Inhibiting Factor), Phenylpyruvate Tautomerase, L-Dopachrome Tautomerase, L-Dopachrome Isomerase, GLIF, MMIF, GIF, Macrophage Migration Inhibitory Factor, Glycosylation-Inhibiting Factor, EC 5.3.3.12, EC 5.3.2.1, Macrophage migration inhibitory factor.
Product # :
CYT-401Price :
Quantity :
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Shipped with Ice Packs
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Description
MIF Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 345 amino acids (1-115 a.a) and having a molecular mass of 39.2kDa. MIF is fused to a 230 amino acid GST-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MIF protein solution (1mg/ml) containing Phosphate Buffered Saline (pH7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
The cytokine Macrophage migration inhibitory factor (MIF) has been identified to be secreted by the pituitary gland and the monocyte/macrophage and to play an important role in endotoxic shock. MIF has the unique property of being released from macrophages and T cells in response to physiological concentrations of glucocorticoids. The secretion of MIF is tightly regulated and decreases at high, anti-inflammatory steroid concentration.
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Synonyms
Macrophage Migration Inhibitory Factor (Glycosylation-Inhibiting Factor), Phenylpyruvate Tautomerase, L-Dopachrome Tautomerase, L-Dopachrome Isomerase, GLIF, MMIF, GIF, Macrophage Migration Inhibitory Factor, Glycosylation-Inhibiting Factor, EC 5.3.3.12, EC 5.3.2.1, Macrophage migration inhibitory factor.
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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
MSPILGYWKI KGLVQPTRLL LEYLEEKYEE HLYERDEGDK WRNKKFELGL EFPNLPYYID GDVKLTQSMA IIRYIADKHN MLGGCPKERA EISMLEGAVL DIRYGVSRIA YSKDFETLKV DFLSKLPEML KMFEDRLCHK TYLNGDHVTH PDFMLYDALD VVLYMDPMCL DAFPKLVCFK KRIEAIPQID KYLKSSKYIA WPLQGWQATF GGGDHPPKSD LVPRGSPEFA MPMFIVNTNV PRASVPDGFL SELTQQLAQA TGKPPQYIAV HVVPDQLMAF GGSSEPCALC SLHSIGKIGG AQNRSYSKLL CGLLAERLRI SPDRVYINYY DMNAANVGWN NSTFA.
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 :
ATPIF1 HumanDescription:
ATPase Inhibitory Factor 1 Human Recombinant
ATPase inhibitor mitochondrial, Inhibitor of F(1)F(o)-ATPase, IF(1), IF1, ATPIF1, ATPI, IP, ATPIP.
Product # :
PRO-1154Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ATPIF1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 106 amino acids (26-106 a.a) and having a molecular mass of 12.2kDa.ATPIF1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ATPIF1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl and 50% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
ATPase inhibitory factor 1 (ATPIF1) attaches to the C-terminal region of a beta subunit of the F1-ATPase at low pH values and, through interference of the beta and gamma subunit interaction, ATPIF1 controls the activity of the F1 (the hydrophilic catalytic core), F0 (the membrane embedded protein channel) ATPase. ATPIF1 overexpression in a number of human carcinomas additionally reinforces its participation in oncogenesis and offers insight into the transformed metabolism of cancer cells, including the reprogramming of energy metabolism in relation to glycolysis. Endogenous F1F(o)-ATPase inhibitor curbing ATP depletion when the mitochondrial membrane potential drops below a threshold and the F1F(o)-ATP synthase begins hydrolyzing ATP to pump protons out of the mitochondrial matrix.
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Synonyms
ATPase inhibitor mitochondrial, Inhibitor of F(1)F(o)-ATPase, IF(1), IF1, ATPIF1, ATPI, IP, ATPIP.
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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
MGSSHHHHHH SSGLVPRGSH MGSHMGSDQS ENVDRGAGSI REAGGAFGKR EQAEEERYFR AQSREQLAAL KKHHEEEIVH HKKEIERLQK EIERHKQKIK MLKHDD.
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 :
EFNA3 HumanDescription:
Ephrin A3 Human Recombinant
Ephrin-A3, EFL2, Ehk1-L, EPLG3, LERK3, EPH-related receptor tyrosine kinase ligand 3.
Product # :
PRO-1460Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
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Description
EFNA3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 217 amino acids (23-214 a.a) and having a molecular mass of 24kDa. EFNA3 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
EFNA3 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
EFNA3 belongs to the ephrin (EPH) family. The ephrins and EPH-related receptors include thelargest subfamily of receptor protein-tyrosine kinases which have been implicated in mediating developmental events, especially in the nervous system and in erythropoiesis. Ephrins are divided into the ephrin-A (EFNA) class and the ephrin-B (EFNB) class, based on their structures and sequence relationships. The Ephrins from the EFNA class are anchored to the membrane by aglycosylphosphatidylinositol linkage, while the others from the EFNB class are transmembrane proteins.
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Synonyms
Ephrin-A3, EFL2, Ehk1-L, EPLG3, LERK3, EPH-related receptor tyrosine kinase ligand 3.
-
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 MGSHMQGPGG ALGNRHAVYW NSSNQHLRRE GYTVQVNVND YLDIYCPHYN SSGVGPGAGP GPGGGAEQYV LYMVSRNGYR TCNASQGFKR WECNRPHAPH SPIKFSEKFQ RYSAFSLGYE FHAGHEYYYI STPTHNLHWK CLRMKVFVCC ASTSHSGEKP VPTLPQFTMG PNVKINVLED FEGENPQVPK LEKSISG
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 :
CCL25 HumanDescription:
Thymus Expressed Chemokine Human Recombinant (CCL25)
C-C motif chemokine 25, Small-inducible cytokine A25, Thymus-expressed chemokine, Chemokine TECK, CCL25, SCYA25, TECK, Ckb15, MGC150327.
Product # :
CHM-364Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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Description
TECK Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 127 amino acids and having a molecular mass of 14.2kDa. The TECK is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Filtered (0.2µm) and lyophilized from a concentrated (1mg/ml) solution in 20mM PB, pH 7.4, 150mM NaCl.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Determined by its ability to chemoattract human monocytes using a concentration range of 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.Citations
More Info
-
Introduction
CCL25 (Teck) is a novel CC chemokine, which is distantly related (about 20% amino acid sequence identity) to other CC chemokines. The mouse CCL25 cDNA has also been cloned and shown to encode a 144 a.a. protein, which exhibits 49% a.a. sequence identity to the human CCL25. Human and mouse CCL25 expression was shown to be greatly restricted to the thymus and small intestine. While dendritic cells are identified as the source of CCL25 production in the thymus, dendritic cells derived from bone marrow do not express CCL25. CCL25 signals through the CCR9 receptor. Teck is possibly involved in T-cell development.
Recombinant human and mouse Teck were shown to be chemotactic for activated macrophages, dendritic cells and thymocytes. The recombinant protein demonstrates chemotactic activity on thymocytes, macrophages, THP-1 cells, and dendritic cells but is inactive on peripheral blood lymphocytes and neutrophils. -
Synonyms
C-C motif chemokine 25, Small-inducible cytokine A25, Thymus-expressed chemokine, Chemokine TECK, CCL25, SCYA25, TECK, Ckb15, MGC150327.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized TECK although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TECK 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.
-
Solubility
It is recommended to reconstitute the lyophilized TECK 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
QGVFEDCCLA YHYPIGWAVL RRAWTYRIQE VSGSCNLPAA IFYLPKRHRK VCGNPKSREV QRAMKLLDAR NKVFAKLHHN MQTFQAGPHA VKKLSSGNSK LSSSKFSNPI SSSRKNVSLL ISANSGL.
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Background
What is the molecular weight/Mw of CCL25 HUMAN Protein?
CCL25 HUMAN Protein has a total Mw of 14.2kDa.
What is the source or expression system of CCL25 HUMAN Protein?
Escherichia Coli.
What is the Purity of CCL25 HUMAN Protein?
CCL25 HUMAN Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of CCL25 HUMAN Protein?
Determined by its ability to chemoattract human monocytes using a concentration range of 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.
What is the amino acid sequence of CCL25 HUMAN Protein?
QGVFEDCCLA YHYPIGWAVL RRAWTYRIQE VSGSCNLPAA IFYLPKRHRK VCGNPKSREV QRAMKLLDAR NKVFAKLHHN MQTFQAGPHA VKKLSSGNSK LSSSKFSNPI SSSRKNVSLL ISANSGL.
What applications can CCL25 HUMAN Protein be used in?
CCL25 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CCL25 HUMAN Protein?
The endotoxin level is minimal, CCL25 HUMAN Protein was purified using conventional chromatography techniques.
Who supplies recombinant CCL25 HUMAN that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.
Where can I order bulk mg quantities of CCL25 HUMAN?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
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 :
ZNHIT1 HumanDescription:
Zinc Finger HIT-Type Containing 1 Human Recombinant
Zinc Finger HIT-Type Containing 1, ZNHIT1, ZNFN4A1, Zinc Finger Protein, Subfamily 4A (HIT Domain Containing) Member 1, Zinc Finger HIT Domain Containing 1, Putative Cyclin G1 Interacting Protein, Cyclin-G1-Binding Protein 1, Zinc Finger Protein Subfamily 4A Member 1, P18 Hamlet, CG1I, H_DJ0747G18.14, p18Hamlet, Zinc Finger HIT Domain-Containing Protein 1, Zinc Finger HIT Type 1, CGBP1.
Product # :
PRO-1448Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ZNHIT1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 177 amino acids (1-154) and having a molecular mass of 19.9kDa. ZNHIT1 is fused to a 23 amino acid His-tag at N-terminus.
Source
Escherichia Coli.
Formulation
The ZNHIT1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Zinc Finger HIT-Type Containing 1 (ZNHIT1) is a member of the ZNHIT1 family and contains 1 HIT-type zinc finger. The ZNHIT1 protein is induced by DNA damage and appears to have a role in p53-mediated apoptosis induction. ZNHIT1 interacts with MAPK11 and MAPK14 and is a component of the chromatin-remodeling SRCAP complex composed of at least SRCAP, DMAP1, RUVBL1, RUVBL2, ACTL6A, YEATS4, ACTR6 and ZNHIT1. ZNHIT1 binds to NR1D2 and discharges it of its inhibitory effect on the transcription of APOC3 without affecting its DNA-binding activity.
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Synonyms
Zinc Finger HIT-Type Containing 1, ZNHIT1, ZNFN4A1, Zinc Finger Protein, Subfamily 4A (HIT Domain Containing) Member 1, Zinc Finger HIT Domain Containing 1, Putative Cyclin G1 Interacting Protein, Cyclin-G1-Binding Protein 1, Zinc Finger Protein Subfamily 4A Member 1, P18 Hamlet, CG1I, H_DJ0747G18.14, p18Hamlet, Zinc Finger HIT Domain-Containing Protein 1, Zinc Finger HIT Type 1, CGBP1.
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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.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMVEKKTS VRSQDPGQRR VLDRAARQRR INRQLEALEN DNFQDDPHAG LPQLGKRLPQ FDDDADTGKK KKKTRGDHFK LRFRKNFQAL LEEQNLSVAE GPNYLTACAG PPSRPQRPFC AVCGFPSPYT CVSCGARYCT VRCLGTHQET RCLKWTV.
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 :
SF20 Mouse, HisDescription:
MYDGF Mouse Recombinant, His Tag
D17Wsu104e, Il25, Ly6elg, MYDGF, Interleukin-25, IL-25, Stromal cell-derived growth factor SF20.
Product # :
CYT-1040Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- sds-page
- Citations
Description
MYDGF Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 165 amino acids (25-166 a.a) and having a molecular mass of 18.1kDa. MYDGF is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MYDGF protein solution (0.5mg/ml) containing 20mM Tris-HCl (pH8.0), 0.1M NaCl and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
sds-page
Citations
More Info
-
Introduction
Myeloid-derived growth factor (Mydgf) is a paracrine-acting protein and a bone marrow-derived monocyte which stimulates cardiac myocyte survival and adaptive angiogenesis for cardiac protection and repair after myocardial infarction. Mydgf induces endothelial cell proliferation through a MAPK1/3-, STAT3- and CCND1-mediated signaling lane. When comparing wild-type mice to mice with a Mydgf-deficiency, the later develop larger infarct scars and more acute contractile dysfunction.
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Synonyms
D17Wsu104e, Il25, Ly6elg, MYDGF, Interleukin-25, IL-25, Stromal cell-derived growth factor SF20.
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Physical Appearance
Sterile Filtered clear 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.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSVSEPTTV PFDVRPGGVV HSFSQDVGPG NKFTCTFTYA SQGGTNEQWQ MSLGTSEDSQ HFTCTIWRPQ GKSYLYFTQF KAELRGAEIE YAMAYSKAAF ERESDVPLKS EEFEVTKTAV SHRPGAFKAE LSKLVIVAKA ARSEL.
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 :
HIF1AN HumanDescription:
Hypoxia-Inducible Factor-1 Alpha Inhibitor Human Recombinant
FIH1, FIH-1, HIF1AN, Factor Inhibiting HIF1A, Hypoxia-inducible factor 1-alpha inhibitor, Hypoxia-inducible factor asparagine hydroxylase, Factor inhibiting HIF-1, FLJ20615, FLJ22027, DKFZp762F1811.
Product # :
PRO-662Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
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Description
HIF1AN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 349 amino acids (1-349) and having a molecular mass of 40.2kDa. The HIF1AN is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein solution (1mg/ml) contains 20mM Tris-HCl pH-8.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Overexpression of the HIF1AN is linked with tumor aggressiveness in pancreatic endocrine tumors. HIF1AN hydroxylates Notch ICD at two residues that are crucial for the function of Notch ICD as a transactivator within cells and during neurogenesis and myogenesis. HIF1AN is commonly expressed in invasive breast carcinoma. The hypoxic response and survival recommends that tumour regulation of HIF1AN is an additional important mechanism for HIF pathway activation. HIF1AN is an asparaginyl hydroxylase enzyme that controls the transcriptional activity of hypoxia-inducible factor. FIH1 is a part of the Fe2+ and 2-oxoglutarate-dependent dioxygenase superfamily, FIH1 is protein that hydoxylates a specific asparagine residue (Asn-803) within the HIF1A C-terminal transactivation domain. In normoxia, the HIF1AN-mediated hydroxylation of the HIF1? transactivation domain which results in blockage of the HIF1A-p300/CBP interaction and represses transcriptional activity of HIF1A targeted genes.
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Synonyms
FIH1, FIH-1, HIF1AN, Factor Inhibiting HIF1A, Hypoxia-inducible factor 1-alpha inhibitor, Hypoxia-inducible factor asparagine hydroxylase, Factor inhibiting HIF-1, FLJ20615, FLJ22027, DKFZp762F1811.
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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
MAATAAEAVA SGSGEPREEA GALGPAWDES QLRSYSFPTR PIPRLSQSDP RAEELIENEE PVVLTDTNLV YPALKWDLEY LQENIGNGDF SVYSASTHKF LYYDEKKMAN FQNFKPRSNR EEMKFHEFVE KLQDIQQRGG EERLYLQQTL NDTVGRKIVM DFLGFNWNWI NKQQGKRGWG QLTSNLLLIG MEGNVTPAHY DEQQNFFAQI KGYKRCILFP PDQFECLYPY PVHHPCDRQS QVDFDNPDYE RFPNFQNVVG YETVVGPGDV LYIPMYWWHH IESLLNGGIT ITVNFWYKGA PTPKRIEYPL KAHQKVAIMR NIEKMLGEAL GNPQEVGPLL NTMIKGRYN.
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 :
Anaplasma Msp5Description:
Anaplasma phagocytophilum Msp5 Recombinant
Major surface protein 5, msp5.
Product # :
PRO-2565Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Anaplasma Msp5 produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 20kDa. Anaplasma Msp5 is expressed with a -6x His tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Sf9 insect cells.
Formulation
Anaplasma Msp5 is supplied at a 20mM HEPES buffer pH-8.0, 200mM NaCl and 20% Glycerol.
Purity
Greater than 80% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
The granulocytic anaplasmosis disease is initiated by the Gram-negative bacterium Anaplasma phagocytophilum. Anaplasma Msp5 is preserved among the Anaplasma classes and expressed in the salivary glands of infected ticks.
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Synonyms
Major surface protein 5, msp5.
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Physical Appearance
Sterile Filtered 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. Avoid multiple freeze-thaw cycles.
-
Immunological Functions
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 :
Anaplasma OmpADescription:
Anaplasma Phagocytophilum OmpA Recombinant
Product # :
PRO-2676Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Anaplasma OmpA produced in E.Coli is a single, non-glycosylated polypeptide chain having a molecular mass of 24kDa. Anaplasma OmpA is expressed with a 10xHis tag and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Anaplasma OmpA is supplied in 20mM HEPES buffer pH-8.0, 200mM NaCl and 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Anaplasma phagocytophilum is a tick-transmitted obligate intracellular bacterium leading to human granulocytic anaplasmosis. Its outer membrane protein A is a peptidoglycan-associated lipoprotein which plays a significant role in the pathogenesis of the disease. OmpA is a part of the porin superfamily sharing a beta-barrel structure.
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Physical Appearance
Sterile Filtered clear 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. Avoid multiple freeze-thaw cycles.
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Immunological Functions
1. Binds IgG-and IgM-type human antibodies.2. immunodot analysis with positive/negative samples.
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Applications
Tested by LAL (Limulus Amoebocyte Lysate) chromogenic endotoxin assay.
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 :
IL2 HumanDescription:
Interleukin-2 Human Recombinant
T-cell growth factor (TCGF), Lymphokine, IL-2.
Product # :
CYT-209Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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- biological activity
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Description
Interleukin-2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 133 amino acids and having a molecular mass of 15.4kDa. The IL-2 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a 0.2μm filtered concentrated solution (1.0mg/ml) in PBS, pH 5.0.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by the dose-dependent stimulation of murine CTLL-2 cells is less than 0.1 ng/ml, corresponding to a Specific Activity of 1x107IU/mg.
Citations
More Info
-
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
T-cell growth factor (TCGF), 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 -18°C. Upon reconstitution IL2 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 Interleukin-2 in sterile distilled water not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
APTSSSTKK TQLQLEHLLL DLQMILNGIN NYKNPKLTRM LTFKFYMPKK ATELKHLQCL EEELKPLEEV LNLAQSKNFH LRPRDLISNI NVIVLELKGS ETTFMCEYAD ETATIVEFLN RWITFCQSII STLT.
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Background
IL 2 HUMAN: A Vital Tool for Advancing Immunotherapy Research
IL 2 HUMAN refers to the human form of Interleukin-2, a critical cytokine in the immune system. This protein is crucial for the growth and activity of T and B lymphocytes, the cells responsible for the body's immune defense against infections.
By promoting the growth of these cells, IL 2 plays a vital role in maintaining and activating the immune response.
Production and Characteristics
Typically, IL 2 is produced through recombinant DNA technology using E. coli bacteria. This method allows for creating large quantities of pure and functional IL 2 protein.
The product appears as a sterile, white lyophilized powder that is non-glycosylated and consists of 133 amino acids with a molecular mass of approximately 15.4 kDa.
Reconstituting IL-2 Human for Laboratory Use
To dissolve the lyophilized IL-2 effectively, it should be reconstituted with sterile distilled water to achieve a minimum 100µg/ml concentration. This makes the protein readily usable for further experimental procedures.
Moreover, the concentration allows for easy adjustment in solubility and ensures optimal conditions for the protein's activity in various research setups. Proper dissolution and storage are crucial to maintain the protein's functionality and stability.
Storage and Stability
The stability of IL 2 is dependent on its storage conditions. When lyophilized, it can remain stable at room temperature for up to three weeks, but for long-term storage, it should be kept desiccated below -18°C.
Once reconstituted, IL 2 should be used within a week if kept at 4°C, or it can be stored at below -18°C for future use. It's important to avoid freeze-thaw cycles, which can degrade the protein.
Purity and Biological Activity
IL 2 HUMAN's purity is generally greater than 97%, confirmed by reverse-phase high-performance liquid chromatography (RP-HPLC) and SDS-PAGE analyses.
Its biological activity is evaluated by its ability to stimulate the proliferation of murine CTLL-2 cells, with an effective dose (ED50) typically less than 0.1 ng/ml. This indicates a very high specific activity, making it highly potent and effective in research settings.
Applications in Research
IL 2 is used extensively in research, particularly in studies focusing on the immune system, autoimmune diseases, and cancer. Furthermore, its role in T-cell growth and function makes it invaluable for developing new therapeutic strategies and understanding immune response mechanisms.
Important Considerations
It is important to remember that IL 2, like all cytokines used in research, is intended for laboratory use only. This protein is not suitable for drug, food, or cosmetic applications. Proper handling and usage instructions must be followed to ensure safety and efficacy in research environments.
Essentially, IL 2 HUMAN is a vital tool in immunological research, offering insights into the complex workings of the immune system and providing avenues for potential therapeutic developments. The careful production, handling, and storage of IL 2 are crucial for its effective use in laboratory settings.
What is the molecular weight/Mw of IL 2 HUMAN Protein?
IL 2 HUMAN Protein has a total Mw of 15.4kDa.
What is the source or expression system of IL 2 HUMAN Protein?
Escherichia Coli.
What is the Purity of IL 2 HUMAN Protein?
IL 2 HUMAN Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of IL 2 HUMAN Protein?
The ED50 as determined by the dose-dependent stimulation of murine CTLL-2 cells is less than 0.1 ng/ml, corresponding to a Specific Activity of 1x107IU/mg.
What is the amino acid sequence of IL 2 HUMAN Protein?
APTSSSTKK TQLQLEHLLL DLQMILNGIN NYKNPKLTRM LTFKFYMPKK ATELKHLQCL EEELKPLEEV LNLAQSKNFH LRPRDLISNI NVIVLELKGS ETTFMCEYAD ETATIVEFLN RWITFCQSII STLT.
What applications can IL 2 HUMAN Protein be used in?
IL 2 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IL 2 HUMAN Protein?
The endotoxin level is minimal, IL 2 HUMAN Protein was purified using conventional chromatography techniques.
Who supplies recombinant IL 2 HUMAN that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.
Where can I order bulk mg quantities of IL 2 HUMAN?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
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 :
IBSP Human, HEKDescription:
Integrin Binding Sialoprotein Human Recombinant, HEK
Integrin Binding Sialoprotein, Integrin-Binding Sialoprotein, Bone Sialoprotein II, Cell-Binding Sialoprotein, BSP II , BNSP, Bone Sialoprotein, BSP-II, SP-II, BSP.
Product # :
PRO-2793Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
IBSP Human Recombinant produced in HEK293 Cells is a single, glycosylated polypeptide chain (17-317 a.a) containing a total of 307 amino acids and having a molecular mass of 34.3 kDa. IBSP is fused to a 6 amino acid His-tag at C-terminus and is purified by proprietary chromatographic techniques.
Source
HEK293 Cells.
Formulation
The IBSP solution (0.5mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
>40%, measured by the ability of the immobilized protein to support the adhesion of MCF7 human breast cancer cells. When cells are added to Human IBSP coated plates 3 ug/ml.
Citations
More Info
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Synonyms
Integrin Binding Sialoprotein, Integrin-Binding Sialoprotein, Bone Sialoprotein II, Cell-Binding Sialoprotein, BSP II , BNSP, Bone Sialoprotein, BSP-II, SP-II, BSP.
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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
FSMKNLHRRV KIEDSEENGV FKYRPRYYLY KHAYFYPHLK RFPVQGSSDS SEENGDDSSE EEEEEEETSN EGENNEESNE DEDSEAENTT LSATTLGYGE DATPGTGYTG LAAIQLPKKA GDITNKATKE KESDEEEEEE EEGNENEESE AEVDENEQGI NGTSTNSTEA ENGNGSSGGD NGEEGEEESV TGANAEDTTE TGRQGKGTSK TTTSPNGGFE PTTPPQVYRT TSPPFGKTTT
VEYEGEYEYT GANEYDNGYE IYESENGEPR GDNYRAYEDE YSYFKGQGYD GYDGQNYYHH QHHHHHH. -
Background
1. Structural Diversity: Research on IBSP often delves into its structural characteristics. IBSP is known for its rich sialic acid content and multiple functional domains, including an RGD cell-binding domain and polyglutamic acid stretches. These structural features enable IBSP to interact with various cells, affecting adhesion and migration.
2. Mineralization Regulator: A significant focus of research is IBSP's role in mineralization. It acts as a nucleator for calcium phosphate crystals, providing a scaffold for bone formation. Understanding how IBSP influences mineralization is crucial for insights into bone health and diseases like osteoporosis.
3. Cell Signaling: Research papers explore IBSP's involvement in cell signaling pathways. IBSP has been linked to angiogenesis, inflammation, and cellular differentiation. Investigating these signaling pathways sheds light on its broader physiological roles.
4. Biomedical Implications: Studies often discuss the biomedical implications of IBSP. Researchers investigate its potential roles in bone disorders such as osteoporosis and periodontal disease. Additionally, IBSP's involvement in tumor metastasis and dental tissue regeneration is a subject of interest.
5. Recombinant IBSP: The use of recombinant IBSP in research is a significant topic. Researchers utilize recombinant IBSP to explore its functions, interactions, and potential therapeutic applications. This allows for controlled experiments and insights into IBSP's behavior.
6. Diagnostics and Therapeutics: Research papers may discuss the diagnostic and therapeutic potential of IBSP. Understanding its roles in health and disease can lead to the development of diagnostic markers and therapeutic interventions, particularly in the context of bone and dental health.
7. Clinical Relevance: Some research may focus on the clinical relevance of IBSP. This could include studies on patient populations with IBSP mutations or alterations, aiming to understand how variations in IBSP may contribute to specific medical conditions.
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 21 HumanDescription:
Interleukin-21 Human Recombinant
Za11, IL-21.
Product # :
CYT-408Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
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- Citations
Description
IL21 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 132 amino acids and having a total molecular mass of 15.4kDa. The IL-21 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from PBS, pH 7.4.
Purity
Greater than 97.0% as determined by SDS-PAGE.
Biological Activity
Measured by its ability to proliferate activated B cells.Citations
More Info
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Introduction
IL-21 is produced by CD4+ T cells in response to antigenic stimulation. Its action enhances antigen-specific responses of immune cells. The biological effects of IL-21 include induction of differentiation of T-cells-stimulated B-cells into plasma cells and memory B-cells, stimulation (in conjuction) with IL-4 of IgG production, and induction of apoptotic effects in naive B-cells and stimulated B-cells in the absence of T-cell signaling. Additionally, IL-21 promotes the anti-tumor activity of CD8+ T-cells and NK cells. IL-21 exerts its effect through binding to a specific type I cytokine receptor, IL-21R, which also contains the gamma chain (°C) found in other cytokine receptors including IL-2, IL-4, IL-7, IL-9 and IL-15. The IL-21/IL-21R interaction triggers a cascade of events which includes activation of the tyrosine kinases JAK1 and JAK3, followed by activation of the transcription factors STAT1 and STAT3.
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Synonyms
Za11, IL-21.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Interleukin-21 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL21 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 Interleukin -21 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
MQDRHMIRMR QLIDIVDQLK NYVNDLVPEF LPAPEDVETN CEWSAFSCFQ KAQLKSANTG NNERIINVSI KKLKRKPPST NAGRRQKHRL TCPSCDSYEK KPPKEFLERF KSLLQKMIHQ HLSSRTHGSE DS.
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 :
CAMP HumanDescription:
Cathelicidin Antimicrobial Peptide Human Recombinant
CAP-18, CAP18, CRAMP, FALL-39, FALL39, HSD26, LL37, 18 kDa cationic antimicrobial protein, FALL-39 peptide antibiotic, Cathelicidin antimicrobial peptide.
Product # :
PRO-1405Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
CAMP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 163 amino acids (34-173 a.a.) and having a molecular mass of 18.4kDa.CAMP is fused to a 23 amino acid His-tag at N-terminus.
Source
Escherichia Coli.
Formulation
CAMP protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
CAMP belongs to the antimicrobial peptide family, contains highly conserved N-terminal signal peptide, a cathelin domain and a structurally variable cationic antimicrobial peptide that produced by extracellular proteolysis from the C-terminus. CAMP has numerous functions besides the antimicrobial activity such as: cell chemotaxis, immune mediator induction and inflammatory response regulation.
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Synonyms
CAP-18, CAP18, CRAMP, FALL-39, FALL39, HSD26, LL37, 18 kDa cationic antimicrobial protein, FALL-39 peptide antibiotic, Cathelicidin antimicrobial peptide.
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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 MGSQVLSYKE AVLRAIDGIN QRSSDANLYR LLDLDPRPTM DGDPDTPKPV SFTVKETVCP RTTQQSPEDC DFKKDGLVKR CMGTVTLNQA RGSFDISCDK DNKRFALLGD FFRKSKEKIG KEFKRIVQRI KDFLRNLVPR TES.
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 :
Inhibin ADescription:
Inhibin Alpha Human Recombinant
Product # :
HOR-303Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
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- source
- formulation
- purity
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Description
Inhibin-Alpha Human Recombinant produced in E.Coli is a non-glycosylated, polypeptide chain containing 264 amino acids comprising of both A and B chains, having a molecular mass of 33.5 kDa.The Inhibin-Alpha is fused with an amino-terminal hexahistidine tag. The Inhibin-Alpha is purified by standard chromatographic techniques.
Source
Escherichia Coli.
Formulation
Inhibin-A alpha chain is supplied in 20mM Tris and 50% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE analysis.
Citations
More Info
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Introduction
Inhibins are dimeric peptide hormones produced by female ovarian granulose cells and male Sertoli cells as well as a variety of other tissues. Inhibins have two isoforms, A and B, with the same alpha subunit but different beta subunits. Inhibin A is a dimer of alpha and beta A subunits, inhibin B is a dimer of alpha and beta B subunits.
Inhibins are thought to inhibit the production of follicle-stimulating hormone (FSH) by the pituitary gland. In addition, Inhibins are also thought to play a role in the control of gametogenesis, and embryonic and fetal development. -
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.Please avoid freeze thaw cycles.
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Amino Acid Sequence
Alpha chain:
STPLMSWPWSPSALRLLQRPPEEPAAHANCHRVALNISFQELGWERWIVYPPSFIFHYCHGGCGLHIP PNLSLPVPGAPPTPAQPYSLLPGAQPCCAALPGTMRPLHVRTTSDGGYSFKYETVPNLLTQHCACI.
Beta Chain:
GLECDGKVNICCKKQFFVSFKDIGWNDWIIAPSGYHANYCEGECPSHIAGTSGSSLSFHSTVINHYRMR
GHSPFANLKSCCVPTKLRPMSMLYYDDGQNIIKKDIQNMIVEECGCS. -
Background
What is the molecular weight/Mw of INHIBIN A Protein?
INHIBIN A Protein has a total Mw of 33.5kDa.
What is the source or expression system of INHIBIN A Protein?
Escherichia Coli.
What is the Purity of INHIBIN A Protein?
INHIBIN A Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of INHIBIN A Protein?
The biological functionality of INHIBIN A Protein will be determined in the future.
What is the amino acid sequence of INHIBIN A Protein?
Alpha chain:
STPLMSWPWSPSALRLLQRPPEEPAAHANCHRVALNISFQELGWERWIVYPPSFIFHYCHGGCGLHIP PNLSLPVPGAPPTPAQPYSLLPGAQPCCAALPGTMRPLHVRTTSDGGYSFKYETVPNLLTQHCACI.
Beta Chain:
GLECDGKVNICCKKQFFVSFKDIGWNDWIIAPSGYHANYCEGECPSHIAGTSGSSLSFHSTVINHYRMR
GHSPFANLKSCCVPTKLRPMSMLYYDDGQNIIKKDIQNMIVEECGCS.
What applications can INHIBIN A Protein be used in?
INHIBIN A Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for INHIBIN A Protein?
The endotoxin level is minimal, INHIBIN A Protein was purified using conventional chromatography techniques.
Who supplies recombinant INHIBIN A that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.
Where can I order bulk mg quantities of INHIBIN A?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
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 :
HIV-1 p24, HisDescription:
HIV-1 p24 Recombinant, His Tag
Product # :
HIV-159Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
HIV-1 p24 His Tag Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 188 amino acids (155-321 a.a.) and having a molecular mass of 21.2 kDa. The HIV-1 p24 is fused to a 21 amino acid His Tag and purified by conventional chromatography.
Source
Escherichia Coli.
Formulation
The HIV-1 p24 protein solution contains 20mM Tris-HCl pH-8, 0.1mM PMSF, 0.1M NaCl and 10% glycerol.
Purity
Greater than 80.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
The HIV1 p24 His Tag protein performs complex orchestrated tasks during the assembly, budding maturation and infection stages of the viral replication cycle. Throughout viral assembly, the proteins form membrane associations and self-associations that ultimately result in budding of an immature virion from the infected cell. HIV-1 P24 gag, the key capsid protein of the HIV-1 virion, is used in clinical trials as one of the components of the HIV-1 vaccine because of the great extent of sequence homology between different isolates.
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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
MGSSHHHHHH SSGLVPRGSH MWVKVVEEKA FSPEVIPMFS ALSEGATPQD LNTMLNTVGG HQAAMQMLKE TINEEAAEWD RLHPVHAGPI APGQMREPRG SDIAGTTSTL QEQIGWMTHN PPIPVGEIYK RWIILGLNKI VRMYSPTSIL DIRQGPKEPF RDYVDRFYKT LRAEQASQEV
KNWMTETL.
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.