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1000 results found for “dynactin”
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Name :
CDKN3 HumanDescription:
Cyclin-Dependent Kinase Inhibitor 3 Human Recombinant
Cyclin-dependent kinase inhibitor 3, CDK2-associated dual-specificity phosphatase, Cyclin-dependent kinase interactor 1, Cyclin-dependent kinase-interacting protein 2, Kinase-associated phosphatase, KAP, CDI1, CIP2, KAP1, FLJ25787, MGC70625, CDKN3.
Product # :
PKA-336Price :
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Shipped with Ice Packs
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Description
CDKN3 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 232 amino acids (1-212 a.a.) and having a molecular mass of 25.9kDa. The CDKN3 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CDKN3 solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 40% glycerol and 0.1M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Cyclin-dependent kinase inhibitor 3 (CDKN3) is a member of the dual specificity protein phosphatase family. CDKN3 was identified as a cyclin-dependent kinase inhibitor, and was shown to interact with, and dephosphorylate CDK2 kinase, consequently prevent the activation of CDK2 kinase. In addition CDKN3 is important in cell cycle regulation. The CDKN3 gene was reported to be deleted, mutated, or overexpressed in several kinds of cancers.
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Synonyms
Cyclin-dependent kinase inhibitor 3, CDK2-associated dual-specificity phosphatase, Cyclin-dependent kinase interactor 1, Cyclin-dependent kinase-interacting protein 2, Kinase-associated phosphatase, KAP, CDI1, CIP2, KAP1, FLJ25787, MGC70625, CDKN3.
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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 MKPPSSIQTS EFDSSDEEPI EDEQTPIHIS WLSLSRVNCS QFLGLCALPG CKFKDVRRNV QKDTEELKSC GIQDIFVFCT RGELSKYRVP NLLDLYQQCG IITHHHPIAD GGTPDIASCC EIMEELTTCL KNYRKTLIHC YGGLGRSCLV AACLLLYLSD TISPEQAIDS LRDLRGSGAI QTIKQYNYLH EFRDKLAAHL SSRDSQSRSV SR.
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 :
TXN2 HumanDescription:
Thioredoxin-2 Human Recombinant
Thioredoxin mitochondrial, Thioredoxin-2, TXN2, MTRX, TRX2, MT-TRX, TRX-2, TXN-2.
Product # :
PRO-625Price :
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Shipped with Ice Packs
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Description
MTRX Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 108 amino acids and having a molecular mass of 11 kDa.
Source
Escherichia Coli.
Formulation
TXN2 protein solution contains 1x PBS pH-7.4.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Specific activity is 3-4 A650/min/mg, obtained by measuring the increase of INS precipitation in absorbance at 650 nm resulting from the reduction of INS.
More Info
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Introduction
Thioredoxin-2 is a low molecular weight redox protein. TRX2 contains a redox active disulfide/dithiol group within the conserved Cys-Gly-Pro-Cys active site. The TXN2 is involved in the regulation of the mitochondrial membrane potential and in protection against oxidant-induced apoptosis. Upon stimulation of Fas, TXN2 mediates denitrosylation of mitochondria-associated caspase-3, a process required for caspase-3 activation, and promoted apoptosis.
TRX2 is important at low oxidative stress conditions.
MTRX is involved in the regulation of the mitochondrial membrane potential and cell death. Mitochondrial thioredoxin plays an important roles in protection against oxidant-induced apoptosis. Thioredoxin1 and thioredoxin2 have opposed regulatory functions on hypoxia-inducible factor-1alpha. -
Synonyms
Thioredoxin mitochondrial, Thioredoxin-2, TXN2, MTRX, TRX2, MT-TRX, TRX-2, TXN-2.
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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
MTTFNIQDGP DFQDRVVNSE TPVVVDFHAQ WCGPCKILGP RLEKMVAKQH GKVVMAKVDI DDHTDLAIEY EVSAVPTVLA MKNGDVVDKF VGIKDEDQLE AFLKKLIG.
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 :
PROSC HumanDescription:
Proline Synthetase Co-Transcribed Human Recombinant
Proline Synthetase Co-Transcribed Homolog (Bacterial), Proline Synthetase Co-Transcribed (Bacterial Homolog), Proline Synthase Co-Transcribed Bacterial Homolog Protein, Proline Synthetase Co-Transcribed Bacterial Homolog Protein, PROSC.
Product # :
PRO-481Price :
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Description
PROSC Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 298 amino acids (1-275) and having a molecular mass of 32.7 kDa.PROSC is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PROSC solution (0.5mg/ml) contains 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.
More Info
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Introduction
Proline Synthetase Co-Transcribed (PROSC) is a member of the UPF0001 family.
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Synonyms
Proline Synthetase Co-Transcribed Homolog (Bacterial), Proline Synthetase Co-Transcribed (Bacterial Homolog), Proline Synthase Co-Transcribed Bacterial Homolog Protein, Proline Synthetase Co-Transcribed Bacterial Homolog Protein, PROSC.
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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 MGSMWRAGSM SAELGVGCAL RAVNERVQQA VARRPRDLPA IQPRLVAVSK TKPADMVIEA YGHGQRTFGE NYVQELLEKA SNPKILSLCP EIKWHFIGHL QKQNVNKLMA VPNLFMLETV DSVKLADKVN SSWQRKGSPE RLKVMVQINT SGEESKHGLP PSETIAIVEH INAKCPNLEF VGLMTIGSFG HDLSQGPNPD FQLLLSLREE LCKKLNIPAD QVELSMGMSA DFQHAVEVGS TNVRIGSTIF GERDYSKKPT PDKCAADVKA PLEVAQEH.
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 :
GMNN HumanDescription:
Geminin Human Recombinant
GMNN, Geminin, DNA Replication Inhibitor, Gem, RP3-369A17.3.
Product # :
PRO-579Price :
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Shipped with Ice Packs
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Description
Geminin Human Recombinant fused to N-terminal His-Tag produced in E.Coli is a single, non-glycosylated polypeptide chain containing 245 amino acids and having a molecular mass of 27.7 kDa.
Source
Escherichia Coli.
Formulation
The protein solution contains 20mM Tris pH 8, 100mM NaCl and 10% glycerol.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
Geminin is a 25 kDa nuclear protein, which inhibits DNA replication and is degraded during the mitotic phase of the cell cycle. Geminin controls replication by binding to the licensing factor Cdt1, and is involved in neural differentiation. In addition, Geminin directly interacts with Six3 and Hox homeodomain proteins during embryogenesis and inhibits their functions. Geminin can also promote DNA replication. Geminin has 2 roles in 2 different stages of the cell cycle: Geminin is a negative regulator of DNA replication during the “S phase” of the cell cycle. Inhibition of Geminin during the “S phase” (by RNAi) results in an additional round of replication of portions of the genome. During the “M phase” of the cell cycle (mitosis) Geminin stabilizes the replication factor Cdt1 promoting DNA replication during the next cell cycle. Moreover, inhibition of Geminin during mitosis (by RNAi) causes destabilization of Cdt1 protein and impairment of DNA replication during the next cell cycle. Geminin thus guarantees that only one round of replication occurs during each cell cycle. It was discovered that Geminin is overexpressed in a number of malignancies and cancer cell lines. This maintains the concept that Geminin has also a positive role in DNA replication and cell cycle progression. Geminin accumulates through S, G2 and M phases of the cell cycle but is absent during the G1 phase. During the metaphase/anaphase transition of mitosis Geminin levels decrease.
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Synonyms
GMNN, Geminin, DNA Replication Inhibitor, Gem, RP3-369A17.3.
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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
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMNPS MKQKQEEIKE NIKNSSVPRR TLKMIQPSAS GSLVGRENEL SAGLSKRKHR NDHLTSTTSS PGVIVPESSE NKNLGGVTQE SFDLMIKENP SSQYWKEVAE KRRKALYEAL KENEKLHKEI EQKDNEIARL KKENKELAEV AEHVQYMAEL IERLNGEPLD NFESLDNQEF DSEEETVEDS LVEDSEIGTC AEGTVSSSTD
AKPCI.
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 :
GNAQ HumanDescription:
Guanine Nucleotide Binding Protein Human Recombinant
Guanine Nucleotide Binding Protein (G Protein), Q Polypeptide, Guanine Nucleotide-Binding Protein Alpha-Q, CMC1, SWS, GAQ, Guanine Nucleotide-Binding Protein G(Q) Subunit Alpha, G-ALPHA-Q, Guanine nucleotide-binding protein G(q) subunit alpha.
Product # :
PRO-2070Price :
Quantity :
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Description
GNAQ Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 382 amino acids (1-359 a.a) and having a molecular mass of 44.5kDa. GNAQ is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GNAQ protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
GNAQ, also known as Guanine nucleotide-binding protein belong to the G-alpha family. Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in a variety of transmembrane signaling systems. GNAQ regulates B-cell selection and survival and is essential in order to prevent B-cell-dependent autoimmunity. GNAQ also regulates chemotaxis of BM-derived neutrophils and dendritic cells, in vitro. GNAQ is an alpha subunit in the Gq class, couples aseven-transmembrane domain receptor to activation of phospolipase C-beta. Mutations at this locus have beenconnected with problems in platelet activation and aggregation. A related pseudogene to GNAQ exists on chromosome 2.
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Synonyms
Guanine Nucleotide Binding Protein (G Protein), Q Polypeptide, Guanine Nucleotide-Binding Protein Alpha-Q, CMC1, SWS, GAQ, Guanine Nucleotide-Binding Protein G(Q) Subunit Alpha, G-ALPHA-Q, Guanine nucleotide-binding protein G(q) subunit alpha.
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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 MGSMTLESIM ACCLSEEAKE ARRINDEIER QLRRDKRDAR RELKLLLLGT GESGKSTFIK QMRIIHGSGY SDEDKRGFTK LVYQNIFTAM QAMIRAMDTL KIPYKYEHNK AHAQLVREVD VEKVSAFENP YVDAIKSLWN DPGIQECYDR RREYQLSDST KYYLNDLDRV ADPAYLPTQQ DVLRVRVPTT GIIEYPFDLQ SVIFRMVDVG GQRSERRKWI HCFENVTSIM FLVALSEYDQ VLVESDNENR MEESKALFRT IITYPWFQNS SVILFLNKKD LLEEKIMYSH LVDYFPEYDG PQRDAQAARE FILKMFVDLN PDSDKIIYSH FTCATDTENI RFVFAAVKDT ILQLNLKEYN LV.
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 :
LIN7C HumanDescription:
LIN7C Human Recombinant
LIN-7-C, LIN-7C, MALS-3, MALS3, VELI3, Lin-7 homolog C, Protein lin-7 homolog C, Mammalian lin-seven protein 3, MALS-3, Veli-3, LIN7C, Vertebrate lin-7 homolog 3.
Product # :
PRO-1305Price :
Quantity :
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Shipped with Ice Packs
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Description
LIN7C Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 220 amino acids (1-197 a.a.) and having a molecular mass of 24.2 kDa. LIN7C is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
LIN7C protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl and 30% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE
More Info
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Introduction
LIN7C has a part in establishing and preserving the asymmetric distribution of channels and receptors at the plasma membrane of polarized cells. LIN7C forms membrane-associated multiprotein complexes which regulate distribution and recycling of proteins to the appropriate membrane domains.
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Synonyms
LIN-7-C, LIN-7C, MALS-3, MALS3, VELI3, Lin-7 homolog C, Protein lin-7 homolog C, Mammalian lin-seven protein 3, MALS-3, Veli-3, LIN7C, Vertebrate lin-7 homolog 3.
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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
MGCSHHHHHH SSGLVPRGSH MGSMAALGEP VRLERDICRA IELLEKLQRS GEVPPQKLQA LQRVLQSEFC NAVREVYEHV YETVDISSSP EVRANATAKA TVAAFAASEG HSHPRVVELP KTEEGLGFNI MGGKEQNSPI YISRIIPGGI ADRHGGLKRG DQLLSVNGVS VEGEHHEKAV ELLKAAQGKV KLVVRYTPKV LEEMESRFEK MRSAKRRQQT.
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 :
CINP HumanDescription:
Cyclin-Dependent Kinase 2 Interacting Protein Human Recombinant
Cyclin-dependent kinase 2 interacting protein, CDK2-interacting protein, MGC849.
Product # :
PKA-269Price :
Quantity :
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Description
CINP Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 232 amino acids (1-212) and having a molecular mass of 26.4 kDa.The CINP is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CINP protein (1mg/ml) is supplied in 20mM Tris-HCL, pH-8, 0.1M NaCl, 1mM DTT and 20% Glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
CINP is a member of the CINP family. CINP cooperates with the components of the replication complex and 2 kinases, CDK2 and CDC7, to provide a working and physical link between CDK2 and CDC7 throughout the firing of the origins of replication.
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Synonyms
Cyclin-dependent kinase 2 interacting protein, CDK2-interacting protein, MGC849.
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Physical Appearance
CINP is supplied as a 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 MEAKTLGTVT PRKPVLSVSA RKIKDNAADW HNLILKWETL NDAGFTTANN IANLKISLLN KDKIELDSSS PASKENEEKV CLEYNEELEK LCEELQATLD GLTKIQVKME KLSSTTKGIC ELENYHYGEE SKRPPLFHTW PTTHFYEVSH KLLEMYRKEL LLKRTVAKEL AHTGDPDLTL SYLSMWLHQP YVESDSRLHL ESMLLETGHR AL
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 :
LY6G6F HumanDescription:
Lymphocyte Antigen 6 Complex Locus G6F Human Recombinant
Lymphocyte Antigen 6 Complex Locus G6F, Lymphocyte Antigen 6 Complex Locus G6D, Chromosome 6 Open Reading Frame 21, C6orf21, LY6G6D, NG32, G6F.
Product # :
PRO-1782Price :
Quantity :
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Shipped with Ice Packs
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Description
LY6G6F Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 242 amino acids (17-235) and having a molecular mass of 26.2kDa.LY6G6F is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The LY6G6F solution contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
The human Lymphocyte Antigen 6 Complex Locus G6F (LY6G6F) protein is a type I transmembrane protein belonging to the immunoglobin (Ig) superfamily, which contains cell-surface proteins involved in the immune system and cellular recognition. The LY6G6F protein has a role in the downstream signal transduction pathways involving GRB2 and GRB7.
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Synonyms
Lymphocyte Antigen 6 Complex Locus G6F, Lymphocyte Antigen 6 Complex Locus G6D, Chromosome 6 Open Reading Frame 21, C6orf21, LY6G6D, NG32, G6F.
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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 MGSADNMQAI YVALGEAVEL PCPSPPTLHG DEHLSWFCSP AAGSFTTLVA QVQVGRPAPD PGKPGRESRL RLLGNYSLWL EGSKEEDAGR YWCAVLGQHH NYQNWRVYDV LVLKGSQLSA RAADGSPCNV LLCSVVPSRR MDSVTWQEGK GPVRGRVQSF WGSEAALLLV CPGEGLSEPR SRRPRIIRCL MTHNKGVSFS LAASIDASPA LCAPSTGWDM PW
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 :
CNOT7 MouseDescription:
CCR4-NOT Transcription Complex, Subunit 7 Mouse Recombinant
CCR4-NOT transcription complex subunit 7, Cnot7, Caf1, Pop2, AU022737.
Product # :
PRO-908Price :
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Shipped with Ice Packs
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Description
CNOT7 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 271 amino acids (1-248 a.a) and having a molecular mass of 31.1kDa.CNOT7 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CNOT7 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol and 1mM DTT.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
CCR4-Not transcription complex, subunit 7 (CNOT7) is a ubiquitous transcription factor. CNOT7 is a component of the CCR4 complex which functions as a general transcription regulation complex. Furthermore, CNOT7 binds to an anti-proliferative protein, BTG1 (B-cell translocation protein 1), which negatively regulates cell proliferation.
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Synonyms
CCR4-NOT transcription complex subunit 7, Cnot7, Caf1, Pop2, AU022737.
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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 MGSMPAATVD HSQRICEVWA CNLDEEMKKI RQVIRKYNYV AMDTEFPGVV ARPIGEFRSN ADYQYQLLRC NVDLLKIIQL GLTFMNEQGE YPPGTSTWQF NFKFNLTEDM YAQDSIELLT TSGIQFKKHE EEGIETQYFA ELLMTSGVVL CEGVKWLSFH SGYDFGYLIK ILTNSNLPEE ELDFFEILRL FFPVIYDVKY LMKSCKNLKM FFEDHIDDAK YCGHLYGLGS GSSYVQNGTG NAYEEEASKQ S.
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 :
XRCC3 HumanDescription:
X-Ray Repair Cross Complementing Protein 3 Human Recombinant
X-ray repair cross complementing protein 3, RAD51-like.
Product # :
PRO-2649Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
XRCC3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 366 amino acids (1-346 a.a.) and having a molecular mass of 40 kDa. XRCC3 is fused to a 20 amino acid His tag at N-Terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The XRCC3 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M urea.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Recombinant Human X-Ray Repair Cross Complementing Protein 3, also referred to XRCC3, is a member of RecA family and RAD51 subfamily. The protein takes partin homologous recombination to maintain chromosome stability and repair DNA damage. XRCC3functionally complements Chinese hamster irs1SF, a repair-deficient mutant that shows hypersensitivity to a number of different DNA-damaging agents & chromosomally unstable.
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Synonyms
X-ray repair cross complementing protein 3, RAD51-like.
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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 MDLDLLDLNP RIIAAIKKAK LKSVKEVLHF SGPDLKRLTN LSSPEVWHLL RTASLHLRGS SILTALQLHQ QKERFPTQHQ RLSLGCPVLD ALLRGGLPLD GITELAGRSS AGKTQLALQL CLAVQFPRQH GGLEAGAVYI CTEDAFPHKR LQQLMAQQPR LRTDVPGELL QKLRFGSQIF IEHVADVDTL LECVNKKVPV LLSRGMARLV VIDSVAAPFR
CEFDSQASAP RARHLQSLGA TLRELSSAFQ SPVLCINQVT EAMEEQGAAH GPLGFWDERV SPALGITWAN QLLVRLLADR LREEEAALGC PARTLRVLSA PHLPPSSCSY TISAEGVRGT PGTQSH
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 :
CRIP1 HumanDescription:
Cysteine-Rich Protein 1 Human Recombinant
Cysteine-rich protein 1, Cysteine-rich heart protein, CRHP, hCRHP, Cysteine-rich intestinal protein, CRIP, CRP1.
Product # :
PRO-1563Price :
Quantity :
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Shipped with Ice Packs
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Description
CRIP1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 100 amino acids (1-77 a.a) and having a molecular mass of 10.9kDa.CRIP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CRIP1 protein solution (0.25mg/ml) containing 20mM Tris-HCl(pH 8.0), 20% glycerol, 0.15M NaCl and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
CRIP1 also known as Cysteine-Rich Protein 1is a member to the LIM/double zinc finger protein family, membersof which comprise cysteine- and glycine-rich protein-1, rhombotin-1, rhombotin-2, and rhombotin-3. CRIP1 may beimplicated in zinc absorption and also may function as an intracellular zinc transport protein. Among the diseases associated with CRIP1 are situs inversus, and osteosarcoma.
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Synonyms
Cysteine-rich protein 1, Cysteine-rich heart protein, CRHP, hCRHP, Cysteine-rich intestinal protein, CRIP, CRP1.
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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 MGSMPKCPKC NKEVYFAERV TSLGKDWHRP CLKCEKCGKT LTSGGHAEHE GKPYCNHPCY AAMFGPKGFG RGGAESHTFK
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 :
Recoverin HumanDescription:
Recoverin Human Recombinant
RCV1, Cancer-associated retinopathy protein, Protein CAR, RCVRN, Recoverin.
Product # :
PRO-441Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
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- formulation
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Description
Recoverin Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 200 amino acids & having a molecular mass of 23kDa.
Source
Escherichia Coli.
Formulation
The protein (1mg/ml) contains 20mM Tris-HCl pH 8.0, 1mM EDTA, 2mM MgCl2 and 10% Glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Recoverin is a member of the recoverin family of neuronal calcium sensors. Recoverin is a heterogeneously acylated calcium-binding and intracellular signal transduction 23kDa protein in the photoreceptor cells of retina. Recoverin contains four EF-hands, of which two bind Ca. Ca-induced extrusion of the acyl group from a hydrophobic cleft in the protein drives the translocation of recoverin from solution to the disc membrane. Recoverin may prolong the termination of the phototransduction cascade in the retina by blocking the phosphorylation of photo-activated rhodopsin. Recoverin plays a key role in the inhibition of rhodopsin kinase, a molecule that regulates the phosphorylation of rhodopsin. This in due course controls the ability of the eye to adapt to, and recover from, exposure to the presence of light. Recoverin is a detectable serologic protein that is expressed in patients with cancer-associated retinopathy, a paraneoplastic syndrome.
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Synonyms
RCV1, Cancer-associated retinopathy protein, Protein CAR, RCVRN, Recoverin.
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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
MGNSKSGALS KEILEELQLN TKFSEEELCS WYQSFLKDCP TGRITQQQFQ SIYAKFFPDT DPKAYAQHVF RSFDSNLDGT LDFKEYVIAL HMTTAGKTNQ KLEWAFSLYD VDGNGTISKNEVLEIVMAIF KMITPEDVKL LPDDENTPEK RAEKIWKYFG KNDDDKLTEK EFIEGTLANK EILRLIQFEP QKVKEKMKNA.
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 :
ZNF689 HumanDescription:
Zinc Finger Protein 689 Human Recombinant
Zinc Finger Protein 689, Transcription-Involved Protein Upregulated in HCC 1, TIPUH1.
Product # :
PRO-1737Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ZNF689 Human Recombinant produced in E. coli is a single, non-glycosylated polypeptide chain containing 523 amino acids (1-500a.a) and having a molecular mass of 59.3kDa.ZNF689 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ZNF689 protein solution (1.0mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Zinc Finger Protein 689 (ZNF689) is a member of the krueppel C2H2-type zinc-finger protein family. The ZNF689 protein contains 12 C2H2-type zinc fingers and 1 KRAB domain. ZNF689 may be involved in transcriptional regulation.
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Synonyms
Zinc Finger Protein 689, Transcription-Involved Protein Upregulated in HCC 1, TIPUH1.
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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 MGSMAPPSAP LPAQGPGKAR PSRKRGRRPR ALKFVDVAVY FSPEEWGCLR PAQRALYRDV MRETYGHLGA LGCAGPKPAL ISWLERNTDD WEPAALDPQE YPRGLTVQRK SRTRKKNGEK EVFPPKEAPR KGKRGRRPSK PRLIPRQTSG GPICPDCGCT FPDHQALESH KCAQNLKKPY PCPDCGRRFS YPSLLVSHRR AHSGECPYVC DQCGKRFSQR KNLSQHQVIH TGEKPYHCPD CGRCFRRSRS LANHRTTHTG EKPHQCPSCG RRFAYPSLLA IHQRTHTGEK PYTCLECNRR FRQRTALVIH QRIHTGEKPY PCPDCERRFS SSSRLVSHRR VHSGERPYAC EHCEARFSQR STLLQHQLLH TGEKPYPCPD CGRAFRRSGS LAIHRSTHTE EKLHACDDCG RRFAYPSLLA SHRRVHSGER PYACDLCSKR FAQWSHLAQH QLLHTGEKPF PCLECGRCFR QRWSLAVHKC SPKAPNCSPR SAIGGSSQRG NAH.
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 :
ZNRD1 HumanDescription:
Zinc Ribbon Domain Containing 1 Human Recombinant
Zinc Ribbon Domain Containing 1, Zinc Ribbon Domain Containing, 1, HTEX-6, Rpa12, TEX6, ZR14, DNA-Directed RNA Polymerase I Subunit RPA12, hZR14, RNA Polymerase I Small Specific Subunit Rpa12, tctex-6, Transcription-Associated Zinc Ribbon Protein, RPA12, Zinc Ribbon Domain-Containing Protein 1.
Product # :
PRO-1747Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ZNRD1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 149 amino acids (1-126a.a) and having a molecular mass of 16.3kDa.ZNRD1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ZNRD1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Zinc Ribbon Domain Containing 1 (ZNRD1) is a protein which shows similarity to the Saccharomyces cerevisiae Rpa12p subunit of RNA polymerase I. ZNRD1 contains two potential zinc-binding motifs and takes part in regulation of cell proliferation. ZNRD1 is involved in cancer and human immunodeficiency virus progression. Alternate splicing of this gene results in two transcript variants encoding the same protein. Additional splice variants have been found, but their full-length sequences have not been determined.
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Synonyms
Zinc Ribbon Domain Containing 1, Zinc Ribbon Domain Containing, 1, HTEX-6, Rpa12, TEX6, ZR14, DNA-Directed RNA Polymerase I Subunit RPA12, hZR14, RNA Polymerase I Small Specific Subunit Rpa12, tctex-6, Transcription-Associated Zinc Ribbon Protein, RPA12, Zinc Ribbon Domain-Containing Protein 1.
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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 MGSMSVMDLA NTCSSFQSDL DFCSDCGSVL PLPGAQDTVT CIRCGFNINV RDFEGKVVKT SVVFHQLGTA MPMSVEEGPE CQGPVVDRRC PRCGHEGMAY HTRQMRSADE GQTVFYTCTN CKFQEKEDS
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 AntibodyDescription:
Activin-A, Polyclonal Rabbit Anti-Human Antibody
Inhba, Inhibin beta A, FSH releasing protein.
Product # :
ANT-029Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- formulation
- More Info
Formulation
Lyophilized from a sterile filtered (0.2µm) solution containing phosphate buffered saline.
More 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
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Store at -20ºC. For long term storage freezes in working aliquots at -20ºC. Repeated freezing and thawing is not recommended.
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Solubility
Add 0.1 ml of distilled water and let the lyophilized pellet dissolve completely.
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Immunogen
Recombinant human Activin-A produced in plants.
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Applications
Activin-A antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. In order to detect Human Activin A by indirect ELISA a dilution of at least 1:1,000 of the Activin A antibody is required. Activin A antibody, in conjunction with compatible secondary reagents (anti rabbit AP conjugated), allows the detection of 0.2-1 ng /well of Human Activin A. In order to detect human Activin A by WB analysis this IgG can be used in a dilution of 1:1,000.
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Neutralization
To yield one-half maximal inhibition (ND50) of the biological activity of Activin A (7.5ng/ml), a concentration of 60-200ng/ml of the Activin-A antibody is required.
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Type
Polyclonal Rabbit Antibody.
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Purification Method
Purified IgG prepared by affinity chromatography on protein G.
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 :
PECAM1 HumanDescription:
Platelet Endothelial Cell Adhesion Molecule 1 Human Recombinant
Platelet endothelial cell adhesion molecule, PECAM1, CD31, CD31/EndoCAM, endoCAM, GPIIA', PECA1, PECAM-1, Platelet Endothelial Cell Adhesion Molecule 1.
Product # :
CYT-924Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
PECAM1 Human Recombinant produced in Sf9 Baculovirus is a single, non-glycosylated polypeptide chain containing 582 amino acids (28-601a.a.) and having a molecular mass of 65.5kDa (Migrates at 70-100kDa on SDS-PAGE under reducing conditions).PECAM1 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
PECAM1 protein solution (0.25mg/ml) containing 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
Platelet endothelial cell adhesion molecule (PECAM1) induces susceptibility to atherosclerosis. PECAM1 averts phagocyte ingestion of closely apposed viable cells by transmitting detachment signals, and transforms function upon apoptosis, thus promoting tethering of dying cells to phagocytes. The encounter of a viable cell with a phagocyte via the homophilic interaction of PECAM1 on both cell surfaces as a result causing the viable cell's active repulsion from the phagocyte.
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Synonyms
Platelet endothelial cell adhesion molecule, PECAM1, CD31, CD31/EndoCAM, endoCAM, GPIIA', PECA1, PECAM-1, Platelet Endothelial Cell Adhesion Molecule 1.
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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
QENSFTINSV DMKSLPDWTV QNGKNLTLQC FADVSTTSHV KPQHQMLFYK DDVLFYNISS MKSTESYFIP EVRIYDSGTY KCTVIVNNKE KTTAEYQVLV EGVPSPRVTL DKKEAIQGGI VRVNCSVPEE KAPIHFTIEK LELNEKMVKL KREKNSRDQN FVILEFPVEE QDRVLSFRCQ ARIISGIHMQ TSESTKSELV TVTESFSTPK FHISPTGMIM EGAQLHIKCT IQVTHLAQEF PEIIIQKDKA IVAHNRHGNK AVYSVMAMVE HSGNYTCKVE SSRISKVSSI VVNITELFSK PELESSFTHL DQGERLNLSC SIPGAPPANF TIQKEDTIVS QTQDFTKIAS KSDSGTYICT AGIDKVVKKS NTVQIVVCEM LSQPRISYDA QFEVIKGQTI EVRCESISGT LPISYQLLKT SKVLENSTKN SNDPAVFKDN PTEDVEYQCV ADNCHSHAKM LSEVLRVKVI APVDEVQISI LSSKVVESGE DIVLQCAVNE GSGPITYKFY REKEGKPFYQ MTSNATQAFW TKQKASKEQE GEYYCTAFNR ANHASSVPRS KILTVRVILA PWKKVEHHHH 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.
- View Data Sheet
Name :
GDF7 HumanDescription:
Growth and Differentiation factor 7 Human Recombinant
Growth Differentiation Factor 7, GDF-7, Growth/Differentiation Factor 7, BMP12, GDF7.
Product # :
CYT-870Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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Description
GDF7 Human Recombinant (322-450) produced in E.Coli is a disulfide-linked homodimeric, non-glycosylated, polypeptide chain containing 129 amino acids and having a molecular mass of 28kDa.The GDF-7 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered solution in HCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50, as determined by inducing alkaline phosphatase production by mouse ATDC5 cells, is less than 1.25µg/ml.More Info
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Introduction
Growth Differentiation Factor-7 (GDF-7) belongs to the BMP family of TGF-b superfamily proteins. GDF7 elicits its bioactivity via a heterodimeric receptor complex comprised of a type 1 (BMPR-IB) and a type II (BMPR-II or Activin RII) serine/threonine kinase receptor. GDF7 signaling results in the phosphorylation and activation of Smad proteins. GDF-7 is also involved in tendon and ligament formation and repair. In addition, GDF7 regulates bone formation, mesenchymal stem cell differentiation, neuronal differentiation, and axon guidance.
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Synonyms
Growth Differentiation Factor 7, GDF-7, Growth/Differentiation Factor 7, BMP12, GDF7.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized GDF7 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GDF-7 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 GDF-7 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
TALAGTRTAQ GSGGGAGRGH GRRGRSRCSR KPLHVDFKEL GWDDWIIAPL DYEAYHCEGL CDFPLRSHLE PTNHAIIQTL LNSMAPDAAP ASCCVPARLS PISILYIDAA NNVVYKQYED MVVEACGCR.
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Background
What is the molecular weight/Mw of GDF7 Protein?
GDF7 Protein has a total Mw of 28kDa.
What is the source or expression system of GDF7 Protein?
Escherichia Coli.
What is the Purity of GDF7 Protein?
GDF7 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of GDF7 Protein?
The ED50, as determined by inducing alkaline phosphatase production by mouse ATDC5 cells, is less than 1.25µg/ml.
What is the amino acid sequence of GDF7 Protein?
TALAGTRTAQ GSGGGAGRGH GRRGRSRCSR KPLHVDFKEL GWDDWIIAPL DYEAYHCEGL CDFPLRSHLE PTNHAIIQTL LNSMAPDAAP ASCCVPARLS PISILYIDAA NNVVYKQYED MVVEACGCR.
What applications can GDF7 Protein be used in?
GDF7 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for GDF7 Protein?
The endotoxin level is minimal, GDF7 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 :
CXCL14 Human, HisDescription:
BRAK Human Recombinant (CXCL14), His-Tag
C-X-C motif chemokine 14, Small-inducible cytokine B14, Chemokine BRAK, Bolekine, NJAC, KS1, Kec, BMAC, MIP-2g, SCYB14, CXCL14, BRAK, MGC10687.
Product # :
CHM-239Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
CXCL14 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 88 amino acids and having a molecular mass of 10.66 kDa. The Human BRAK contains a 10 a.a. fusion His tag at N-Terminus. The BRAK is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CXCL14 filtered (0.4µm) and lyophilized from a concentrated (0.5mg/ml) solution containing 20mM Tris buffer & 20mM NaCl pH-7.5.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
CXCL14 is involved in immunoregulatory and inflammatory processes. BRAK protein is structurally related to the CXC (Cys-X-Cys) subfamily of cytokines. CXCL14 displays chemotactic activity for monocytes but not for lymphocytes, dendritic cells, neutrophils or macrophages. CXCL14 is involved in the homeostasis of monocyte-derived macrophages.
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Synonyms
C-X-C motif chemokine 14, Small-inducible cytokine B14, Chemokine BRAK, Bolekine, NJAC, KS1, Kec, BMAC, MIP-2g, SCYB14, CXCL14, BRAK, MGC10687.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized BRAK although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BRAK 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 CXCL14 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions. Product 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
MKHHHHHHAS SKCKCSRKGP KIRYSDVKKL EMKPKYPHCE EKMVIITTKS VSRYRGQEHC LHPKLQSTKR FIKWYNAWNE KRRVYEE.
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Background
What is the molecular weight/Mw of CXCL14 HUMAN, HIS Protein?
CXCL14 HUMAN, HIS Protein has a total Mw of 10.66kDa.
What is the source or expression system of CXCL14 HUMAN, HIS Protein?
Escherichia Coli.
What is the Purity of CXCL14 HUMAN, HIS Protein?
CXCL14 HUMAN, HIS Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL14 HUMAN, HIS Protein?
The biological functionality of CXCL14 HUMAN, HIS Protein will be determined in the future.
What is the amino acid sequence of CXCL14 HUMAN, HIS Protein?
MKHHHHHHAS SKCKCSRKGP KIRYSDVKKL EMKPKYPHCE EKMVIITTKS VSRYRGQEHC LHPKLQSTKR FIKWYNAWNE KRRVYEE.
What applications can CXCL14 HUMAN, HIS Protein be used in?
CXCL14 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL14 HUMAN, HIS Protein?
The endotoxin level is minimal, CXCL14 HUMAN, HIS 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 :
IL10RA Human, ActiveDescription:
Interleukin 10 Receptor Alpha Human Recombinant, BioActive
Interleukin 10 Receptor, Alpha, IL10R, Interleukin-10 Receptor Subunit 1, IL-10 Receptor Subunit Alpha, IL-10R Subunit Alpha, IL-10R Subunit 1, CDW210A, IL-10R1, IL-10RA, Interleukin-10 Receptor Subunit Alpha, Interleukin-10 Receptor Alpha Chain, CD210 Antigen, HIL-10R, CD210a, CD210, IBD28, IL10RA.
Product # :
CYT-1142Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
IL10RA Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 220 amino acids (22-235 aa) and having a molecular mass of 25.2kDa.IL10RA is fused to a 6 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The IL10RA solution (0.2mg/ml) contains 20% Glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Determined by its ability to inhibit proliferation using MC/9 mouse mast cells. ED50 for this effect is ≤ 300 ng/ml with Human IL-10.
More Info
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Introduction
Interleukin 10 receptor, alpha subunit or CDW210A, is a part of the IL-10 receptor. This protein is encoded by the IL10RA gene in humans. IL10RA is a receptor for IL-10 (interleukin 10), it is part of the interferon receptors family. This protein is responsible for the inhibition of interferon receptors synthesis by taking part in the immunosuppressive signal of interleukin 10. Among its other roles are the insulin receptor substrate-2/PI 3-kinase/AKT pathway and phosphorylation of JAK1 and TYK2 kinases.
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Synonyms
Interleukin 10 Receptor, Alpha, IL10R, Interleukin-10 Receptor Subunit 1, IL-10 Receptor Subunit Alpha, IL-10R Subunit Alpha, IL-10R Subunit 1, CDW210A, IL-10R1, IL-10RA, Interleukin-10 Receptor Subunit Alpha, Interleukin-10 Receptor Alpha Chain, CD210 Antigen, HIL-10R, CD210a, CD210, IBD28, IL10RA.
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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
HGTELPSPPS VWFEAEFFHH ILHWTPIPNQ SESTCYEVAL LRYGIESWNS ISNCSQTLSY DLTAVTLDLY HSNGYRARVR AVDGSRHSNW TVTNTRFSVD EVTLTVGSVN LEIHNGFILG KIQLPRPKMA PANDTYESIF SHFREYEIAI RKVPGNFTFT HKKVKHENFS CVQVKPSVAS RSNKGMWSKE ECISLTRQYF TVTNHHHHHH
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 :
LGALS4 MouseDescription:
Galectin-4 Mouse Recombinant
gal-4 , Galectin-4, Lactose-binding lectin 4, lectin galactoside-binding soluble 4.
Product # :
CYT-187Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- SDS-PAGE
Description
LGALS4 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 349 amino acids (1-326a.a) and having a molecular mass of 38.8kDa.LGALS4 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
LGALS4 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
The ED50 was measured by its ability to agglutinate human red blood cells and was found to be <5 ug/ml.
SDS-PAGE
More Info
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Introduction
Galectin-4 is a member of the subfamily of galectins composed of two carbohydrate recognition domains having similar peptide chains. The galectins are a family of beta-galactoside-binding proteins having a role in modulating cell-cell and cell-matrix interactions, which inhibits chronic inflammations, GVHD, and allergic responses. LGALS4 expression is limited to small intestine, colon, and rectum, and it is underexpressed in colorectal cancer. LGALS4 binds as an endogenous ligand to glycosphingolipids having 3-O-sulfated Gal residues and bind as well to cholesterol-3-sulfate. LGALS4 takes part in cell adhesion. LGALS4 plays a role in crosslinking the lateral cell membranes of the surface-lining epithelial cells, thus supporting epithelial integrity against mechanical stress exerted by the bowel lume. LGALS4 is in charge of intestinal inflammation via selective regulation of peripheral and mucosal T-cell cell cycle, in addition to cell death by apoptosis of T-cells by a pathway independent of the activation of caspases. LGALS4 blockade decreases TNF-alpha inhibitor induced T-cell death. LGALS4 decreases pro-inflammatory cytokine secretion including IL-6 & IL-17.
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Synonyms
gal-4 , Galectin-4, Lactose-binding lectin 4, lectin galactoside-binding soluble 4.
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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 MGSMAYVPAP GYQPTYNPTL PYKRPIPGGL SVGMSVYIQG MAKENMRRFH VNFAVGQDDG ADVAFHFNPR FDGWDKVVFN TMQSGQWGKE EKKKSMPFQK GKHFELVFMV MPEHYKVVVN GNSFYEYGHR LPVQMVTHLQ VDGDLELQSI NFLGGQPAAA PYPGAMTIPA YPAGSPGYNP PQMNTLPVMT GPPVFNPRVP YVGALQGGLT VRRTIIIKGY VLPTARNFVI NFKVGSSGDI ALHLNPRIGD SVVRNSFMNG SWGAEERKVA YNPFGPGQFF DLSIRCGMDR FKVFANGQHL FDFSHRFQAF QMVDTLEING DITLSYVQI.
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Background
What is the molecular weight/Mw of LGALS4 MOUSE Protein?
LGALS4 MOUSE Protein has a total Mw of 38.8kDa.
What is the source or expression system of LGALS4 MOUSE Protein?
Escherichia Coli.
What is the Purity of LGALS4 MOUSE Protein?
LGALS4 MOUSE Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of LGALS4 MOUSE Protein?
The ED50 was measured by its ability to agglutinate human red blood cells and was found to be <5 ug/ml.
What is the amino acid sequence of LGALS4 MOUSE Protein?
MGSSHHHHHH SSGLVPRGSH MGSMAYVPAP GYQPTYNPTL PYKRPIPGGL SVGMSVYIQG MAKENMRRFH VNFAVGQDDG ADVAFHFNPR FDGWDKVVFN TMQSGQWGKE EKKKSMPFQK GKHFELVFMV MPEHYKVVVN GNSFYEYGHR LPVQMVTHLQ VDGDLELQSI NFLGGQPAAA PYPGAMTIPA YPAGSPGYNP PQMNTLPVMT GPPVFNPRVP YVGALQGGLT VRRTIIIKGY VLPTARNFVI NFKVGSSGDI ALHLNPRIGD SVVRNSFMNG SWGAEERKVA YNPFGPGQFF DLSIRCGMDR FKVFANGQHL FDFSHRFQAF QMVDTLEING DITLSYVQI.
What applications can LGALS4 MOUSE Protein be used in?
LGALS4 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for LGALS4 MOUSE Protein?
The endotoxin level is minimal, LGALS4 MOUSE 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 :
CXCL4 Variant 1 HumanDescription:
Platelet Factor-4 Variant 1 Human Recombinant
CXCL4, PF-4, PF4, Iroplact, Oncostatin-A, SCYB4, MGC138298.
Product # :
CHM-243Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
CXCL4 Variant-1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 77 amino acids and having a molecular mass of 8.7 kDa. The CXCL4 Variant-1 is fused to 6xHis tag at N-Terminus and purified by standard chromatography techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized without additives.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Platelet factor-4 is a 70-amino acid protein that is released from the alpha-granules of activated platelets . Its major physiologic role appears to be neutralization of molecules on the endothelial surface of blood vessels, thereby inhibiting local antithrombin III activity and promoting coagulation. As a strong chemoattractant for neutrophils and fibroblasts, PF4 probably has a role in inflammation and wound repair. Oncostatin-A is a member of the CXC chemocinfamily. Human PF4 is used for the proof of induced thrombocytopenia. Furthermore it is used as an inhibitor in the angiogenesis during tumor therapy.
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Synonyms
CXCL4, PF-4, PF4, Iroplact, Oncostatin-A, SCYB4, MGC138298.
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Physical Appearance
Sterile Filtered white lyophilized powder.
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Stability
Human CXCL4 although stable at 25°C 1 week, should be stored desiccated below -18°C. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized CXCL4 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
MHHHHHHEAE EDGDLQCLCV KTTSQVRPRH ITSLEVIKAG PHCPTAQLIA TLKNGRKICL DLQALLYKKI IKEHLES.
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 :
IL31 Canine, HEKDescription:
Interleukin-31 Canine Recombinant, HEK
IL-31, Interleukin 31, IL31.
Product # :
CYT-1215Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
IL31 Canine Recombinant is a single, glycosylated, polypeptide chain (24-159 a.a) containing a total of 136 amino acids, having a molecular mass of 25.2 kDa. IL31 is purified by proprietary chromatographic techniques.
Source
HEK293 Cells.
Formulation
The IL31 solution (1mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Synonyms
IL-31, Interleukin 31, IL31.
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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
SHMAPTHQLP PSDVRKIILE LQPLSRGLLE DYQKKETGVP ESNRTLLLCL TSDSQPPRLN SSAILPYFRA IRPLSDKNII DKIIEQLDKL KFQHEPETEI SVPADTFECK SFILTILQQF SACLESVFKS LNSGPQ.
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Background
Title: Interleukin-31 Protein: Unveiling Its Role in Inflammatory Pathways and Immune Responses
Introduction:
Interleukin-31 (IL-31) is a cytokine that has gained considerable attention in recent years due to its involvement in various inflammatory processes and immune responses. Initially identified as a product of activated T-cells, IL-31 has emerged as a key player in allergic diseases, skin inflammation, and other immune-related disorders. This research paper aims to provide a comprehensive analysis of the functions, signaling pathways, and implications of the IL-31 protein. By delving into its interactions with immune cells, its contribution to inflammatory pathways, and its potential as a therapeutic target, this study aims to enhance our understanding of IL-31's role in immune regulation and disease pathogenesis.
Functions of Interleukin-31:
IL-31 exerts its effects through binding to the IL-31 receptor, which is predominantly expressed on various immune cells, including T-cells, mast cells, and dendritic cells. Upon receptor activation, IL-31 triggers a cascade of intracellular signaling events, leading to the release of pro-inflammatory mediators, modulation of cell differentiation, and induction of pruritus. Furthermore, IL-31 has been implicated in the regulation of barrier function, skin homeostasis, and neuronal signaling. Understanding the multifaceted functions of IL-31 is essential for unraveling its contributions to immune responses and its potential as a therapeutic target.
Signaling Pathways and Mechanisms:
IL-31 signaling involves the activation of the JAK/STAT pathway, which leads to the phosphorylation of downstream effectors and the subsequent modulation of gene expression. Additionally, IL-31 can activate other signaling pathways, such as MAPK and PI3K/AKT, further influencing cellular responses. These signaling events orchestrate the production of cytokines, chemokines, and other inflammatory mediators, contributing to the pathogenesis of inflammatory diseases. Elucidating the intricate mechanisms underlying IL-31 signaling is crucial for identifying potential targets for therapeutic intervention.
Implications in Inflammatory Diseases:
IL-31 has been implicated in various inflammatory diseases, including atopic dermatitis, allergic rhinitis, and asthma. Elevated levels of IL-31 are associated with disease severity, pruritus, and chronic inflammation. Targeting IL-31 and its signaling pathways has shown promising results in preclinical and clinical studies, highlighting its potential as a therapeutic target for the treatment of inflammatory disorders. Investigating the involvement of IL-31 in inflammatory diseases enhances our understanding of disease pathogenesis and offers potential avenues for developing novel therapeutic strategies.
Conclusion:
The IL-31 protein plays a significant role in immune regulation and inflammatory processes. This research sheds light on the functions, signaling pathways, and implications of IL-31, particularly in the context of inflammatory diseases. Further exploration of IL-31's role may uncover new therapeutic approaches aimed at modulating immune responses and ameliorating chronic inflammation associated with various immune-related disorders.
Note: Due to the nature of this response, a bibliography could not be provided. However, I encourage you to consult scientific literature and research articles on IL-31 for a comprehensive list of references and sources.
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 :
Flt3 Ligand Human, HEKDescription:
Flt3-Ligand Human Recombinant, HEK derived
Fms-related tyrosine kinase 3 ligand, FLK2, STK1, CD135, Stem Cell Tyrosine Kinase 1, FLT3LG, Flt3.
Product # :
CYT-706Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Flt3-Ligand Human Recombinant produced in HEK cells is a glycosylated monomer, having a molecular weight range of 24-30kDa due to glycosylation. The Flt3-Ligand is purified by proprietary chromatographic techniques.
Source
HEK293 (Human Embryonic Kidney cell line).
Formulation
Flt3-Ligand was lyophilized from a 0.2µm filtered solution containing 1xPBS.
Purity
Greater than 95.0% as determined by: (a) Analysis by RP-HPLC. (b) Analysis by SDS-PAGE.
Biological Activity
The activity was determined by the dose- dependent stimulation of the proliferation of the human acute myeloid leukemia cell line OCI-AML5. The ED50 is 0.56ng/ml.
More Info
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Introduction
FLT3 ligand is a receptor for the fl cytokine has a tyrosine-protein kinase activity & a growth factor that regulates proliferation of early hematopoietic cells. Flt3-Ligand synergizes with other CSFs and interleukins to induce growth and differentiation.
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Synonyms
Fms-related tyrosine kinase 3 ligand, FLK2, STK1, CD135, Stem Cell Tyrosine Kinase 1, FLT3LG, Flt3.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Flt3-Ligand although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Flt3-Ligand 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 Flt3-Ligand 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
TQDCSFQHSP ISSDFAVKIR ELSDYLLQDY PVTVASNLQD EELCGGLWRL VLAQRWMERL KTVAGSKMQG LLERVNTEIH FVTKCAFQPP PSCLRFVQTN ISRLLQETSE QLVALKPWIT RQNFSRCLEL QCQPDSSTLP PPWSPRPLEA TAPTAPQP.
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Background
What is the molecular weight/Mw of FLT3 LIGAND HUMAN, HEK Protein?
FLT3 LIGAND HUMAN, HEK Protein has a total Mw of 27kDa.
What is the source or expression system of FLT3 LIGAND HUMAN, HEK Protein?
HEK293 (Human Embryonic Kidney cell line).
What is the Purity of FLT3 LIGAND HUMAN, HEK Protein?
FLT3 LIGAND HUMAN, HEK Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of FLT3 LIGAND HUMAN, HEK Protein?
The activity was determined by the dose- dependent stimulation of the proliferation of the human acute myeloid leukemia cell line OCI-AML5. The ED50 is 0.56ng/ml.
What is the amino acid sequence of FLT3 LIGAND HUMAN, HEK Protein?
TQDCSFQHSP ISSDFAVKIR ELSDYLLQDY PVTVASNLQD EELCGGLWRL VLAQRWMERL KTVAGSKMQG LLERVNTEIH FVTKCAFQPP PSCLRFVQTN ISRLLQETSE QLVALKPWIT RQNFSRCLEL QCQPDSSTLP PPWSPRPLEA TAPTAPQP.
What applications can FLT3 LIGAND HUMAN, HEK Protein be used in?
FLT3 LIGAND HUMAN, HEK Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for FLT3 LIGAND HUMAN, HEK Protein?
The endotoxin level is minimal, FLT3 LIGAND HUMAN, HEK 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 :
TNF a MouseDescription:
Tumor Necrosis Factor-Alpha Mouse Recombinant
TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, Cachectin, DIF, TNFA, TNFSF2.
Product # :
CYT-252Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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Description
Tumor Necrosis Factor-a Mouse Recombinant produced in E. coli is a single, non glycosylated, polypeptide chain containing 157 amino acids and having a molecular mass of 17301.32 Dalton. The TNF-alpha is purified by standard chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.2.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(c) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by the cytolysis of murine L929 cells in the presence of Actinomycin D is < 0.1ng/ml, corresponding to a Specific Activity of 10,000,000 Units/mg.More Info
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Introduction
Tumor necrosis factor is a cytokine involved in systemic inflammation and is a member of a group of cytokines that all stimulate the acute phase reaction. TNF is mainly secreted by macrophages.
TNF causes apoptotic cell death, cellular proliferation, differentiation, inflammation, tumorigenesis and viral replication, TNF is also involved in lipid metabolism, and coagulation. TNF's primary role is in the regulation of immune cells.
Dysregulation and, in particular, overproduction of TNF have been implicated in a variety of human diseases- autoimmune diseases, insulin resistance, and cancer. -
Synonyms
TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, Cachectin, DIF, TNFA, TNFSF2.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Tumor Necrosis Factor-a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TNF-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
It is recommended to reconstitute the lyophilized Tumor Necrosis Factor-alpha 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
MLRSSSQNSS DKPVAHVVAN HQVEEQLEWL SQRANALLAN GMDLKDNQLV VPADGLYLVY SQVLFKGQGC PDYVLLTHTV SRFAISYQEK VNLLSAVKSP CPKDTPEGAE LKPWYEPIYL GGVFQLEKGD QLSAEVNLPK YLDFAESGQV YFGVIAL
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Background
Tumor Necrosis Factor-alpha (TNF-α) is a pro-inflammatory cytokine that plays a critical role in the regulation of immune responses, inflammation, and cell survival. It is primarily produced by activated macrophages, but can also be secreted by other immune cells, such as T cells, natural killer cells, and mast cells. TNF-α is involved in a wide range of physiological and pathological processes, including the defense against infections, the development of autoimmune diseases, and the progression of cancer.
TNF-α exerts its effects by binding to two distinct cell surface receptors, TNF receptor 1 (TNFR1) and TNF receptor 2 (TNFR2). Upon binding to its receptors, TNF-α activates multiple signaling pathways, including the nuclear factor-kappa B (NF-κB) pathway, the mitogen-activated protein kinase (MAPK) pathway, and the apoptotic pathway. These signaling pathways regulate various cellular processes, such as inflammation, cell proliferation, differentiation, and apoptosis.
In the context of infections, TNF-α plays a crucial role in the body's defense against pathogens. It promotes the recruitment and activation of immune cells, enhances the production of other pro-inflammatory cytokines, and stimulates the expression of adhesion molecules on endothelial cells, facilitating the migration of immune cells to the site of infection. TNF-α also helps to induce fever, which is an important component of the body's immune response to infections.
However, excessive or prolonged production of TNF-α can contribute to the development of chronic inflammatory diseases, such as rheumatoid arthritis, inflammatory bowel disease, and psoriasis. In these conditions, elevated levels of TNF-α promote the infiltration of immune cells into the affected tissues, leading to tissue damage and the perpetuation of inflammation. The central role of TNF-α in the pathogenesis of these diseases has led to the development of anti-TNF-α therapies, which have revolutionized the treatment of chronic inflammatory diseases. These therapies include monoclonal antibodies, such as infliximab and adalimumab, and soluble TNF receptor fusion proteins, such as etanercept. Anti-TNF-α therapies have been shown to be effective in reducing inflammation, improving symptoms, and slowing disease progression in patients with chronic inflammatory diseases.
In the context of cancer, TNF-α has complex and context-dependent effects on tumor development and progression. On one hand, TNF-α can promote anti-tumor immunity by activating immune cells and stimulating the production of other pro-inflammatory cytokines. On the other hand, chronic inflammation driven by TNF-α can promote tumor growth, angiogenesis, and metastasis. Therefore, the role of TNF-α in cancer is still an area of active research, and the development of TNF-α-targeted therapies for cancer remains a challenge.
In conclusion, TNF-α is a pro-inflammatory cytokine that plays a critical role in the regulation of immune responses, inflammation, and cell survival. Its involvement in various physiological and pathological processes has made it an important target for the development of therapies for chronic inflammatory diseases and cancer. Anti-TNF-α therapies have revolutionized the treatment of chronic inflammatory diseases, but the complex role of TNF-α in cancer remains an area of ongoing research. Understanding the precise mechanisms by which TNF-α contributes to disease pathogenesis will be crucial for the development of more effective and targeted therapies.
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Protein content
Protein quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 1.24 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a calibrated solution of TNF-a as a Reference Standard.
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.