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1000 results found for “Ferritin”
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Name :
C8G HumanDescription:
Complement Component 8, Gamma Human Recombinant
Complement component 8 gamma polypeptide, C8C, complement component C8 gamma chain, MGC142186.
Product # :
PRO-947Price :
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Description
C8G Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 203 amino acids (21-202) and having a molecular mass of 22.6 kDa.The C8G is fused to a 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The C8G solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 0.15M NaCl and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
C8, a component of the complement system consists of three polypeptides C8A, C8B and C8G and takes part in the formation of Membrane Attack Complex (MAC). Patients with C8 deficiency are exposed to several bacteria infections. C8G, a member of the lipocalin family and calycin superfamily, is a secreted protein that can bind retinol. C8G is created in the liver, monocytes and fibroblast and has a role in clearing pathogens from an infected host.
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Synonyms
Complement component 8 gamma polypeptide, C8C, complement component C8 gamma chain, MGC142186.
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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 MQKPQRPRRP ASPISTIQPK ANFDAQQFAG TWLLVAVGSA CRFLQEQGHR AEATTLHVAP QGTAMAVSTF RKLDGICWQV RQLYGDTGVL GRFLLQARGA RGAVHVVVAE TDYQSFAVLY LERAGQLSVK LYARSLPVSD SVLSGFEQRV QEAHLTEDQI FYFPKYGFCE AADQFHVLDE VRR
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 :
TECK Human, HisDescription:
Thymus Expressed Chemokine (CCL25) Human Recombinant, His Tag
C-C motif chemokine 25, Small-inducible cytokine A25, Thymus-expressed chemokine, Chemokine TECK, CCL25, SCYA25, TECK, Ckb15, MGC150327.
Product # :
CHM-032Price :
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Description
TECK Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 152 amino acids (24-150 a.a.) and having a molecular mass of 16.8kDa.TECK is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
TECK protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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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
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 MGSHMQGVFE DCCLAYHYPI GWAVLRRAWT YRIQEVSGSC NLPAAIFYLP KRHRKVCGNP KSREVQRAMK LLDARNKVFA KLHHNTQTFQ AGPHAVKKLS SGNSKLSSSK FSNPISSSKR NVSLLISANS GL.
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 :
CALR HumanDescription:
Calreticulin Human Recombinant
cC1qR, CRT, FLJ26680, RO, SSA, CRP55, Calreticulin, ERp60, CRTC, CALR.
Product # :
PRO-813Price :
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Description
CALR Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 421 amino acids (18-417 a.a.) and having a molecular mass of 48.7 kDa. CALR protein is fused to a 21 amino acid His-Tag at N-terminus and purified by standard chromatography.
Source
Escherichia Coli.
Formulation
CALR Human solution containing 20mM Tris-HCl pH-8, 1mM DTT, 0.1M NaCl and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
CALR is a multifunctional protein that acts as a main Ca(2+)-binding (storage) protein in the lumen of the endoplasmic reticulum. Calreticulin is localized in the nucleus, and participates in transcription regulation. Calreticulin binds to the synthetic peptide KLGFFKR, which is nearly identical to an amino acid sequence in the DNA-binding domain of the superfamily of nuclear receptors. CALR binds to antibodies in specific sera of systemic lupus and Sjogren patients which have anti-Ro/SSA antibodies, it is well conserved among species, and it is positioned in the endoplasmic and sarcoplasmic reticulum where it binds calcium. The amino terminus of CALR interacts with the DNA-binding domain of the glucocorticoid receptor and prevents the receptor from binding to its specific glucocorticoid response element. CALR reduces the binding of androgen receptor to its hormone-responsive DNA element and inhibits androgen receptor and retinoic acid receptor transcriptional activities in vivo, as well as retinoic acid-induced neuronal differentiation. Therefore, CALR acts as a significant modulator of the regulation of gene transcription by nuclear hormone receptors.
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Synonyms
cC1qR, CRT, FLJ26680, RO, SSA, CRP55, Calreticulin, ERp60, CRTC, CALR.
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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 MEPAVYFKEQ FLDGDGWTSR WIESKHKSDF GKFVLSSGKF YGDEEKDKGL QTSQDARFYA LSASFEPFSN KGQTLVVQFT VKHEQNIDCG GGYVKLFPNS LDQTDMHGDS EYNIMFGPDI CGPGTKKVHV IFNYKGKNVL INKDIRCKDD EFTHLYTLIV RPDNTYEVKI DNSQVESGSL EDDWDFLPPK KIKDPDASKP EDWDERAKID DPTDSKPEDW DKPEHIPDPD AKKPEDWDEE MDGEWEPPVI QNPEYKGEWK PRQIDNPDYK GTWIHPEIDN PEYSPDPSIY AYDNFGVLGL DLWQVKSGTI FDNFLITNDE AYAEEFGNET WGVTKAAEKQ MKDKQDEEQR LKEEEEDKKR KEEEEAEDKE DDEDKDEDEE DEEDKEEDEE EDVPGQAKDE L.
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 :
FHL2 HumanDescription:
Four And A Half LIM Domains 2 Human Recombinant
AAG11, DRAL, FHL-2, SLIM-3, SLIM3, Four and a half LIM domains protein 2, LIM domain protein DRAL, Skeletal muscle LIM-protein 3, FHL2, RNA Binding Motif Protein 18, RNA-Binding Motif Protein 18, RBM18.
Product # :
PRO-2110Price :
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Description
FHL2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 302 amino acids (1-279 a.a) and having a molecular mass of 34.6kDa. FHL2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
FHL2 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Four And A Half LIM Domains 2 (FHL2) belongs to the four-and-a-half-LIM-only protein family. Family members are comprised of 2 highly conserved, tandemly arranged, zinc finger domains with 4 highly conserved cysteines binding a zinc atom in each zinc finger. The FHL2 protein is assumed to play a part in the assembly of extracellular membranes. Furthermore, FHL2 is down-regulated during transformation of normal myoblasts to rhabdomyosarcoma cells and the FHL2 functions as a link between presenilin-2 and an intracellular signaling pathway.
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Synonyms
AAG11, DRAL, FHL-2, SLIM-3, SLIM3, Four and a half LIM domains protein 2, LIM domain protein DRAL, Skeletal muscle LIM-protein 3, FHL2, RNA Binding Motif Protein 18, RNA-Binding Motif Protein 18, RBM18.
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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 MGSMTERFDC HHCNESLFGK KYILREESPY CVVCFETLFA NTCEECGKPI GCDCKDLSYK DRHWHEACFH CSQCRNSLVD KPFAAKEDQL LCTDCYSNEY SSKCQECKKT IMPGTRKMEY KGSSWHETCF ICHRCQQPIG TKSFIPKDNQ NFCVPCYEKQ HAMQCVQCKK PITTGGVTYR EQPWHKECFV CTACRKQLSG QRFTARDDFA YCLNCFCDLY AKKCAGCTNP ISGLGGTKYI SFEERQWHND CFNCKKCSLS LVGRGFLTER DDILCPDCGK DI.
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 :
GRXB E.ColiDescription:
Glutaredoxin-2 E.Coli Recombinant
Glutaredoxin-2, Grx2, grxB, b1064, JW1051.
Product # :
ENZ-130Price :
Quantity :
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Description
GRXB produced in E.Coli is a single, non-glycosylated polypeptide chain containing 235 amino acids (1-215 a.a.) and having a molecular mass of 26.5kDa.GRXB is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GRXB protein solution (1mg/ml) 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 50mM NaCl.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Glutaredoxin-2 (GrxB) is amember of the glutaredoxin family. Glutaredoxins are small redox enzymes of approximately 100 amino-acid residues which use glutathione as a cofactor. Glutaredoxins are oxidized by substrates, and reduced non-enzymatically by glutathione. GrxB is involved in reducing some disulfides in a coupled system with glutathione reductase. GrxB doesn’t act as hydrogen donor for ribonucleotide reductase.
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Synonyms
Glutaredoxin-2, Grx2, grxB, b1064, JW1051.
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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 MKLYIYDHCP YCLKARMIFG LKNIPVELHV LLNDDAETPT RMVGQKQVPI LQKDDSRYMP ESMDIVHYVD KLDGKPLLTG KRSPAIEEWL RKVNGYANKL LLPRFAKSAF DEFSTPAARK YFVDKKEASA GNFADLLAHS DGLIKNISDD LRALDKLIVK PNAVNGELSE DDIQLFPLLR NLTLVAGINW PSRVADYRDN MAKQTQINLL SSMAI.
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 :
VCPKMT HumanDescription:
Valosin Containing Protein Lysine Methyltransferase Human Recombinant
Valosin Containing Protein Lysine (K) Methyltransferase, Methyltransferase-Like Protein 21D, VCP Lysine Methyltransferase, Protein-Lysine Methyltransferase METTL21D, Chromosome 14 Open Reading Frame 138, C14orf138, METTL21D, VCP-KMT, EC 2.1.1.- .
Product # :
PRO-2145Price :
Quantity :
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Description
VCPKMT Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 252 amino acids (1-229 a.a.) and having a molecular mass of 28.2kDa.VCPKMT is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
VCPKMT protein solution (1mg/ml) containing 20mM Phosphate buffer saline (pH 8.0), 1mM DTT and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
VCPKMT is a member of the methyltransferase superfamily. VCPKMT is a protein-lysine N-methyltransferase which specifically trimethylates 'Lys-315' of VCP/p97; this alteration reduces VCP ATPase activity.
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Synonyms
Valosin Containing Protein Lysine (K) Methyltransferase, Methyltransferase-Like Protein 21D, VCP Lysine Methyltransferase, Protein-Lysine Methyltransferase METTL21D, Chromosome 14 Open Reading Frame 138, C14orf138, METTL21D, VCP-KMT, EC 2.1.1.- .
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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
MGSSHHHHHH SSGLVPRGSH MGSMADTLES SLEDPLRSFV RVLEKRDGTV LRLQQYSSGG VGCVVWDAAI VLSKYLETPE FSGDGAHALS RRSVLELGSG TGAVGLMAAT LGADVVVTDL EELQDLLKMN INMNKHLVTG SVQAKVLKWG EEIEGFPSPP DFILMADCIY YEESLEPLLK TLKDISGFET CIICCYEQRT MGKNPEIEKK YFELLQLDFD FEKIPLEKHD EEYRSEDIHI IYIRKKKSKF PS
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 :
RALY HumanDescription:
RALY Human Recombinant
RALY Heterogeneous Nuclear Ribonucleoprotein, RNA-Binding Protein (Autoantigenic, HnRNP-Associated With Lethal Yellow), HnRNP Associated With Lethal Yellow Protein Homolog, Heterogeneous Nuclear Ribonucleoprotein C-Like 2, HnRNP Core Protein C-Like 2, Autoantigen P542, HNRPCL2, P542, RNA Binding Protein, Autoantigenic (HnRNP-Associated With Lethal Yellow Homolog (Mouse)), RNA Binding Protein, Autoantigenic (HnRNP-Associated With Lethal Yellow Homolog), RNA-Binding Protein (Autoantigenic), RNA-Binding Protein Raly, RNA-binding protein Raly.
Product # :
PRO-2095Price :
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Description
RALY Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 329 amino acids (1-306 a.a) and having a molecular mass of 34.9kDa. RALY is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
RALY protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
RALY belongs to the heterogeneous nuclear ribonucleoprotein (hnRNP) gene family. RALY takes part in pre-mRNA splicing and also in embryonic development. Moreover, alternate splicing results in multiple transcript variants have been found for RALY.
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Synonyms
RALY Heterogeneous Nuclear Ribonucleoprotein, RNA-Binding Protein (Autoantigenic, HnRNP-Associated With Lethal Yellow), HnRNP Associated With Lethal Yellow Protein Homolog, Heterogeneous Nuclear Ribonucleoprotein C-Like 2, HnRNP Core Protein C-Like 2, Autoantigen P542, HNRPCL2, P542, RNA Binding Protein, Autoantigenic (HnRNP-Associated With Lethal Yellow Homolog (Mouse)), RNA Binding Protein, Autoantigenic (HnRNP-Associated With Lethal Yellow Homolog), RNA-Binding Protein (Autoantigenic), RNA-Binding Protein Raly, RNA-binding protein Raly.
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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 MGSMSLKLQA SNVTNKNDPK SINSRVFIGN LNTALVKKSD VETIFSKYGR VAGCSVHKGY AFVQYSNERH ARAAVLGENG RVLAGQTLDI NMAGEPKPDR PKGLKRAASA IYSGYIFDYD YYRDDFYDRL FDYRGRLSPV PVPRAVPVKR PRVTVPLVRR VKTNVPVKLF ARSTAVTTSS AKIKLKSSEL QAIKTELTQI KSNIDALLSR LEQIAAEQKA NPDGKKKGDG GGAGGGGGGG GSGGGGSGGG GGGGSSRPPA PQENTTSEAG LPQGEARTRD DGDEEGLLTH SEEELEHSQD TDADDGALQ.
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 :
CRABP2 HumanDescription:
Cellular Retinoic Acid binding Protein 2 Human Recombinant
RBP6, CRABP-II, CRABP2, RETINOIC ACID-BINDING PROTEIN CELLULAR TYPE II, Cellular retinoic acid-binding protein 2, Cellular retinoic acid-binding protein II.
Product # :
PRO-637Price :
Quantity :
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Shipped with Ice Packs
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Description
CRABP2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 136 amino acids and having a molecular mass of 15.6 kDa. The CRABP2 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CRABP2 protein solution contains 20mM Tris-HCl pH-8 and 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
CRABP2 NCBI Accession No: NP_001869 regulates the access of retinoic acid to the nuclear retinoic acid receptors. CRABP2 is involved in a regulatory feedback mechanism that controls the action of retinoic acid on cell differentiation.
CRABP2 is involved in the conversion of vitamin A into its intracellular active form retinoic acid, which regulate the genes responsible for lipid metabolism and adipocyte differentiation. CRABP2 gene is located on chromosome 1q21-23 and this region has been linked with related disorders such as familial combined hyperlipidemia (FCHL) and type 2 diabetes mellitus.
CRABP proteins are of low molecular weight having an important function in retinoic acid-mediated regulation of human skin growth and differentiation. -
Synonyms
RBP6, CRABP-II, CRABP2, RETINOIC ACID-BINDING PROTEIN CELLULAR TYPE II, Cellular retinoic acid-binding protein 2, Cellular retinoic acid-binding protein II.
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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
MPNFSGNWKI IRSENFEELL KVLGVNVMLR KIAVAAASKP AVEIKQEGDT FYIKTSTTVR TTEINFKVGE EFEEQTVDGR PCKSLVKWES ENKMVCEQKL LKGEGPKTSW TRELTNDGEL ILTMTADDVV CTRVYVRE.
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 :
ZCCHC12 HumanDescription:
Zinc Finger, CCHC Domain Containing 12 Human Recombinant
PNMA7A, SIZN, SIZN1, Zinc finger CCHC domain-containing protein 12, Smad-interacting zinc finger protein 1, ZCCHC12.
Product # :
PRO-1982Price :
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Description
ZCCHC12 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 425 amino acids (1-402 a.a) and having a molecular mass of 47.8kDa. ZCCHC12 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ZCCHC12 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Zinc Finger, CCHC Domain Containing 12 (ZCCHC12) which holds 1 CCHC-type zinc finger is a part of the ZCCHC12 family. ZCCHC12 takes part in the bone morphogenetic protein (BMP)-signaling pathway as a transcriptional coactivator. BMP signaling is positively modulated as a result of the interaction between ZCCHC12 with SMAD1 and the association with CBP in the transcription complex.
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Synonyms
PNMA7A, SIZN, SIZN1, Zinc finger CCHC domain-containing protein 12, Smad-interacting zinc finger protein 1, ZCCHC12.
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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 MGSMASIIAR VGNSRRLNAP LPPWAHSMLR SLGRSLGPIM ASMADRNMKL FSGRVVPAQG EETFENWLTQ VNGVLPDWNM SEEEKLKRLM KTLRGPAREV MRVLQATNPN LSVADFLRAM KLVFGESESS VTAHGKFFNT LQAQGEKASL YVIRLEVQLQ NAIQAGIIAE KDANRTRLQQ LLLGGELSRD LRLRLKDFLR MYANEQERLP NFLELIRMVR EEEDWDDAFI KRKRPKRSES MVERAVSPVA FQGSPPIVIG SADCNVIEID DTLDDSDEDV ILVESQDPPL PSWGAPPLRD RARPQDEVLV IDSPHNSRAQ FPSTSGGSGY KNNGPGEMRR ARKRKHTIRC SYCGEEGHSK ETCDNESDKA QVFENLIITL QELTHTEMER SRVAPGEYND FSEPL.
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 :
RNF7 HumanDescription:
Ring Finger Protein 7 Human Recombinant
RING-box protein 2 isoform 1, Ring finger protein 7, CKBBP1, ROC2, SAG, RING-box protein 2, Rbx2, CKII beta-binding protein 1, Regulator of cullins 2, Sensitive to apoptosis gene protein, RBX2, RNF7.
Product # :
PRO-1671Price :
Quantity :
Shipping Method :
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Description
RNF7 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 136 amino acids (1-113 a.a) and having a molecular mass of 15.1kDa.RNF7 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
RNF7 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Ring Finger Protein 7, also known as RNF7, is an extremely conserved ring finger protein. RNF7 is a vital subunit of SKP1-cullin/CDC53-F box protein ubiquitin ligases that are a part of the protein degradation machinery important for cell cycle progression and signal transduction. RNF7 is a substrate of casein kinase II (CSNK2A1/CKII) and also interacts with it. The phosphorylation of RNF7 by CSNK2A1 promotes the degradation of IkappaBalpha (CHUK/IKK-alpha/IKBKA) and p27Kip1(CDKN1B).
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Synonyms
RING-box protein 2 isoform 1, Ring finger protein 7, CKBBP1, ROC2, SAG, RING-box protein 2, Rbx2, CKII beta-binding protein 1, Regulator of cullins 2, Sensitive to apoptosis gene protein, RBX2, RNF7.
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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 MGSMADVEDG EETCALASHS GSSGSKSGGD KMFSLKKWNA VAMWSWDVEC DTCAICRVQV MDACLRCQAE NKQEDCVVVW GECNHSFHNC CMSLWVKQNN RCPLCQQDWV VQRIGK.
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 :
DHRS4 HumanDescription:
Dehydrogenase/Reductase Member 4 Human Recombinant
Dehydrogenase/reductase SDR family member 4, NADPH-dependent carbonyl reductase/NADP-retinol dehydrogenase, CR, PHCR, NADPH-dependent retinol dehydrogenase/reductase, NRDR, humNRDR, Peroxisomal short-chain alcohol dehydrogenase, PSCD, SCAD-SRL, Short-chain dehydrogenase/reductase family member 4, DHRS4, SDR-SRL, SDR25C1, SDR25C2.
Product # :
ENZ-207Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
DHRS4 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 302 amino acids (1-278) and having a molecular mass of 32.1kDa.DHRS4 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The DHRS4 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH7.5), 20% glycerol and 1mM DTT.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Dehydrogenase/reductase SDR family member 4 (DHRS4) is a member of the short-chain dehydrogenases/reductases (SDR) family. DHRS4 reduces all trans retinal and 9-cis retinal. In addition, the DHRS4 protein can catalyze the oxidation of all trans retinol with NADP as cofactor, but with a much lower efficiency. Furthermore, DHRS4 reduces alkyl phenyl ketones and alpha dicarbonyl compounds with aromatic rings, such as pyrimidine 4 aldehyde, 3 benzoylpyridine, 4 benzoylpyridine, menadione and 4 hexanoylpyridine.
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Synonyms
Dehydrogenase/reductase SDR family member 4, NADPH-dependent carbonyl reductase/NADP-retinol dehydrogenase, CR, PHCR, NADPH-dependent retinol dehydrogenase/reductase, NRDR, humNRDR, Peroxisomal short-chain alcohol dehydrogenase, PSCD, SCAD-SRL, Short-chain dehydrogenase/reductase family member 4, DHRS4, SDR-SRL, SDR25C1, SDR25C2.
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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 MGSHMHKAGL LGLCARAWNS VRMASSGMTR RDPLANKVAL VTASTDGIGF AIARRLAQDG AHVVVSSRKQ QNVDQAVATL QGEGLSVTGT VCHVGKAEDR ERLVATAVKL HGGIDILVSN AAVNPFFGSI MDVTEEVWDK TLDINVKAPA LMTKAVVPEM EKRGGGSVVI VSSIAAFSPS PGFSPYNVSK TALLGLTKTL AIELAPRNIR VNCLAPGLIK TSFSRMLWMD KEKEESMKET LRIRRLGEPE DCAGIVSFLC SEDASYITGE TVVVGGGTPS RL.
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-10 Human, Sf9Description:
Interleukin 10 Human Recombinant, Sf9, Active
Interleukin-10, IL-10, Cytokine synthesis inhibitory factor, CSIF, IL10, GVHDS, IL10A, TGIF, T-Cell Growth Inhibitory Factor.
Product # :
CYT-1147Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
IL-10 Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 166 amino acids (19-178 aa) and having a molecular mass of 19.4kDa. IL-10 is fused to a 6 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The IL-10 solution (0.5mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Measured in a cell proliferation assay using MC/9 mouse mast cells. The ED50 range < 5 ng/ml.
More Info
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Introduction
Interleukin 10 or IL-10 or human cytokine synthesis inhibitory factor, is a cytokine (anti-inflammatory). IL10 gene is coding for il-10 In humans. Interleukin 10 has a receptor complex that is built from a couple of IL-10 receptor-1 and a couple of IL-10 receptor-2 proteins. therfore, the whole receptor unit consists of four IL-10 receptor molecules. IL-10 binds the receptor and causes STAT3 signalling through the phosphorylation of the cytoplasmic ends of IL-10 receptor 1 and IL-10 receptor 2 through JAK1 and Tyk2.
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Synonyms
Interleukin-10, IL-10, Cytokine synthesis inhibitory factor, CSIF, IL10, GVHDS, IL10A, TGIF, T-Cell Growth Inhibitory Factor.
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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
SPGQGTQSEN SCTHFPGNLP NMLRDLRDAF SRVKTFFQMK DQLDNLLLKE SLLEDFKGYL GCQALSEMIQ FYLEEVMPQA ENQDPDIKAH VNSLGENLKT LRLRLRRCHR FLPCENKSKA VEQVKNAFNK LQEKGIYKAM SEFDIFINYI EAYMTMKIRN HHHHHH.
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 :
CXCL8 Human, GSTDescription:
Interleukin-8 (1-72) (CXCL8) Human Recombinant, GST Tag
Interleukin-8, IL-8, C-X-C motif chemokine 8, IL8, CXCL8
Product # :
CHM-047Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Human Interleukin-8 produced in E. coli containing 72 amino acids.Recombinant Human Interleukin-8 is fused to GST tag at its N-terminus and purified by proprietary chromatographic technique.
Source
Escherichia Coli.
Formulation
IL8 GST solution contains 25mM Tris-Base/ 25mM K2CO3.
Purity
Protein is >95% pure as determined by 10% PAGE (coomassie staining).
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
Interleukin-8, IL-8, C-X-C motif chemokine 8, IL8, CXCL8
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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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Applications
Immunoassay.
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Background
What is the source or expression system of CXCL8 HUMAN, GST Protein?
Escherichia Coli.
What is the Purity of CXCL8 HUMAN, GST Protein?
CXCL8 HUMAN, GST Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL8 HUMAN, GST Protein?
The biological functionality of CXCL8 HUMAN, GST Protein will be determined in the future.
What is the amino acid sequence of CXCL8 HUMAN, GST Protein?
CXCL8 HUMAN, GST Protein is composed from 72 amino acids.
What applications can CXCL8 HUMAN, GST Protein be used in?
CXCL8 HUMAN, GST Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL8 HUMAN, GST Protein?
The endotoxin level is minimal, CXCL8 HUMAN, GST 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 :
Adiponectin ProteinDescription:
Adiponectin Human Recombinant
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
Product # :
CYT-280Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- sds-page
Description
The Adiponectin Human recombinant protein is a single, non-glycosilated polypeptide chain produced in E. coli, having a molecular weight of 25.1 kDa and containing 231 amino acids (15-244).
Source
Escherichia Coli.
Formulation
Acrp30 protein solution contains Phosphate buffered saline pH 7.4 and 1mM DTT.
Purity
Acrp30 purity is greater than 90% as determined by SDS-PAGE.
sds-page
More Info
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Introduction
The adipose tissue exclusively expresses and secretes Adiponectin (Acrp30). Acrp30 is involved in various physiological processes such as energy homeostasis, insulin sensitivity, hormonal processes, fatty acid metabolism and obesity.
Adiponectin circulates in the plasma. Decreased levels of Adiponectin are associated with insulin resistance and hyperinsulinemia, as seen in people with obesity insulin resistance, and diabetes type 2, whose plasma levels of adiponectin are reduced.
The modular structure of Acrp30 is comprised of N-terminal collagenous domain followed by a C-terminal globular domain.
Acrp30 also acts as a significant negative regulator in hematopoiesis and immune systems; it may be involved in ending inflammatory responses through its inhibitory functions. Adiponectin inhibits endothelial NF-kappa-b signaling through a cAMP-dependent pathway, it also inhibits TNF-alpha- induced expression of endothelial adhesion molecules. -
Synonyms
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
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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
MGHDQETTTQGPGVLLPLPKGACTGWMAGIPGHPGHNGAPGRDGRDGTPGE
KGEKGDPGLIGPKGDIGETGVPGAEGPRGFPGIQGRKGEPGEGAYVYRSAFSV
GLETYVTIPNMPIRFTKIFYNQQNHYDGSTGKFHCNIPGLYYFAYHITVYMKD
VKVSLFKKDKAMLFTYDQYQENNVDQASGSVLLHLEVGDQVWLQVYGEGE
RNGLYADNDNDSTFTGFLLYHDTN. -
Background
Adiponectin Human Recombinant: Unraveling its Potential in Therapeutic Applications
1. Abstract
This paper aims to deliver an extensive exploration into Adiponectin Human Recombinant, a vital adipokine implicated in a multitude of metabolic processes. By delving into the structure, biological roles, and signaling pathways of adiponectin, we elucidate its contribution to pathophysiological conditions. Moreover, we examine the potential therapeutic application of adiponectin in metabolic and cardiovascular diseases.
2. Introduction
Adiponectin, a protein predominantly secreted by adipose tissue, plays an integral part in regulating metabolic processes such as glucose regulation and fatty acid oxidation. Understanding the intricacies of adiponectin's actions could pave the way for innovative therapeutic interventions in diseases like obesity, diabetes, and cardiovascular disease.
3. Structure and Signaling of Adiponectin
Adiponectin is a 30kDa protein consisting of a collagen-like domain and a C-terminal globular domain. It signals through adiponectin receptors AdipoR1 and AdipoR2, which then activate several intracellular signaling pathways, including AMP-activated protein kinase (AMPK) and peroxisome proliferator-activated receptor-alpha (PPAR-α), regulating various metabolic processes.
4. Biological Functions of Adiponectin
Adiponectin has been shown to enhance insulin sensitivity, stimulate fatty acid oxidation, and exert anti-inflammatory effects. Additionally, it is involved in regulating energy homeostasis and has been linked to the regulation of food intake and body weight.
5. Adiponectin in Disease Pathology
Reduced levels of adiponectin have been associated with obesity, insulin resistance, type 2 diabetes, and cardiovascular disease. Moreover, adiponectin deficiency has been observed in metabolic syndrome, emphasizing the adipokine's crucial role in metabolic health.
6. Therapeutic Potential of Adiponectin
Given adiponectin's role in metabolic regulation, its potential as a therapeutic target is of considerable interest. Approaches to increase circulating adiponectin levels or enhance adiponectin signaling could offer potential therapeutic strategies for managing metabolic diseases and cardiovascular conditions.
7. Conclusion and Future Perspectives
While our understanding of adiponectin and its role in health and disease has greatly advanced in recent years, there is still much to uncover. Further research on the precise molecular mechanisms of adiponectin could pave the way for novel therapeutic approaches.
What is the molecular weight / Mw of ADIPONECTIN Protein?
ADIPONECTIN Protein has a total Mw of 25.1kDa.
What is the source or expression system of ADIPONECTIN Protein?
Escherichia Coli.
What is the Purity of ADIPONECTIN Protein?
ADIPONECTIN Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of ADIPONECTIN Protein?
The biological functionality of ADIPONECTIN Protein will be determined in the future.
What is the amino acid sequence of ADIPONECTIN Protein?
MGHDQETTTQGPGVLLPLPKGACTGWMAGIPGHPGHNGAPGRDGRDGTPGE
KGEKGDPGLIGPKGDIGETGVPGAEGPRGFPGIQGRKGEPGEGAYVYRSAFSV
GLETYVTIPNMPIRFTKIFYNQQNHYDGSTGKFHCNIPGLYYFAYHITVYMKD
VKVSLFKKDKAMLFTYDQYQENNVDQASGSVLLHLEVGDQVWLQVYGEGE
RNGLYADNDNDSTFTGFLLYHDTN..
What applications can ADIPONECTIN Protein be used in?
ADIPONECTIN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for ADIPONECTIN Protein?
The endotoxin level is minimal, ADIPONECTIN 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 :
ACVR1 HumanDescription:
Activin A Receptor Type 1 Human Recombinant
ACVR1A, ALK2, ACVR1, ACTRI, ACTR-I, ACVRLK2, FOP, SKR1, TSRI, Activin receptor type I, Activin receptor-like kinase 2, ALK-2, TSR-I, Serine/threonine-protein kinase receptor R1, TGF-B superfamily receptor type I.
Product # :
CYT-1140Price :
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Shipped with Ice Packs
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Description
ACVR1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 342 amino acids (21-123a.a.) and having a molecular mass of 38.4kDa. ACVR1 is expressed with a 239 amino acid hIgG-His-Tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
ACVR1 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
sds-page
More Info
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Introduction
Activin A Receptor Type 1 (ACVR1) is a member of TGF-beta serine/threonine kinase receptor family. ACVR1 forms a receptor complex contains2 type II and 2 type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate,bind and activate SMAD transcriptional regulators. ACVR1 takes part in left-right pattern formation during embryogenesis and is also essential in the BMP pathway which is responsible for the development and repair of the skeletal system.ACVR1 is linked to Fibrodysplasia Ossificans Progressiva which isknown for the formation of heterotopic bone throughout the body.
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Synonyms
ACVR1A, ALK2, ACVR1, ACTRI, ACTR-I, ACVRLK2, FOP, SKR1, TSRI, Activin receptor type I, Activin receptor-like kinase 2, ALK-2, TSR-I, Serine/threonine-protein kinase receptor R1, TGF-B superfamily receptor type I.
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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
MEDEKPKVNP KLYMCVCEGL SCGNEDHCEG QQCFSSLSIN DGFHVYQKGC FQVYEQGKMT
CKTPPSPGQA VECCQGDWCN RNITAQLPTK GKSFPGTQNF HLELEPKSCD KTHTCPPCPA
PELLGGPSVF LFPPKPKDTL MISRTPEVTC VVVDVSHEDP EVKFNWYVDG VEVHNAKTKP
REEQYNSTYR VVSVLTVLHQ DWLNGKEYKC KVSNKALPAP IEKTISKAKG QPREPQVYTL
PPSRDELTKN QVSLTCLVKG FYPSDIAVEW ESNGQPENNY KTTPPVLDSD GSFFLYSKLT
VDKSRWQQGN VFSCSVMHEA LHNHYTQKSL SLSPGKHHHH HH. -
Background
Functional Implications and Therapeutic Prospects of Activin A Receptor Type 1 Human Recombinant
1. Abstract
This study illuminates the functional roles and potential therapeutic applications of Activin A Receptor Type 1 Human Recombinant (ACVR1), a crucial protein in the TGF-beta superfamily signaling pathway. Through a comprehensive review of its structure, signaling mechanism, biological functions, and disease associations, this paper aims to elucidate the current understanding of ACVR1 and its potential therapeutic implications in various disease states.
2. Introduction
The Activin A Receptor Type 1 Human Recombinant, abbreviated as ACVR1, is a receptor protein vital for transmitting cellular signals in the Transforming Growth Factor-beta (TGF-beta) superfamily pathway. Known to play pivotal roles in organogenesis, bone growth, and cell differentiation, the ACVR1 and its functions present vast therapeutic potential.
3. Structure and Signaling of ACVR1
ACVR1 is a transmembrane serine/threonine kinase receptor, characterized by an extracellular ligand-binding domain and an intracellular kinase domain for signal transduction. Binding of ligands such as Activin A leads to the formation of heteromeric complexes with type II receptors, triggering phosphorylation events that activate downstream signaling pathways.
4. Biological Functions of ACVR1
Being a part of the TGF-beta superfamily signaling pathway, ACVR1 is implicated in a broad spectrum of biological processes. It is crucial for embryonic development, cellular proliferation, differentiation, apoptosis, and homeostasis. It also plays a significant role in bone morphogenesis, contributing to skeletal patterning and growth.
5. ACVR1 in Disease Pathology
The dysregulation of ACVR1 has been associated with various pathological conditions, including Fibrodysplasia Ossificans Progressiva (FOP), a rare genetic disorder characterized by progressive ossification of soft tissues. Mutations in ACVR1 lead to enhanced BMP signaling, causing aberrant bone formation. This highlights the critical role of ACVR1 in skeletal homeostasis and disease.
6. Therapeutic Potential of ACVR1
Given the central role of ACVR1 in cellular signaling and its association with disease, it presents a promising target for therapeutic intervention. Strategies to modulate ACVR1 signaling could potentially ameliorate symptoms of diseases like FOP, offering promising avenues for novel therapeutic approaches.
7. Conclusion and Future Perspectives
While our understanding of ACVR1's functional roles has expanded significantly over the years, much remains to be elucidated. Further research into the precise molecular mechanisms of ACVR1 and its pathway will pave the way for therapeutic advances, enhancing our capability to combat various diseases.
What is the molecular weight / Mw of ACVR1 Protein?
ACVR1 Protein has a total Mw of 38.4kDa.
What is the source or expression system of ACVR1 Protein?
Sf9, Baculovirus cells.
What is the Purity of ACVR1 Protein?
ACVR1 Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of ACVR1 Protein?
The biological functionality of ACVR1 Protein will be determined in the future.
What is the endotoxin level for ACVR1 Protein?
The endotoxin level is minimal, ACVR1 Protein was purified using conventional chromatography techniques.
What is the amino acid sequence of ACVR1 Protein?
MEDEKPKVNP KLYMCVCEGL SCGNEDHCEG QQCFSSLSIN DGFHVYQKGC FQVYEQGKMT
CKTPPSPGQA VECCQGDWCN RNITAQLPTK GKSFPGTQNF HLELEPKSCD KTHTCPPCPA
PELLGGPSVF LFPPKPKDTL MISRTPEVTC VVVDVSHEDP EVKFNWYVDG VEVHNAKTKP
REEQYNSTYR VVSVLTVLHQ DWLNGKEYKC KVSNKALPAP IEKTISKAKG QPREPQVYTL
PPSRDELTKN QVSLTCLVKG FYPSDIAVEW ESNGQPENNY KTTPPVLDSD GSFFLYSKLT
VDKSRWQQGN VFSCSVMHEA LHNHYTQKSL SLSPGKHHHH HH.
What applications can ACVR1 Protein be used in?
ACVR1 Protein can probably be used in western blot, ELISA and Lateral Flow
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
GDNF Human, Sf9Description:
Glial-Derived Neurotrophic Factor Human Recombinant, Sf9
Glial cell line-derived neurotrophic factor, hGDNF, Astrocyte-derived trophic factor, ATF, ATF1, ATF2, HFB1-GDNF, HSCR3.
Product # :
CYT-1162Price :
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Description
GDNF Human Recombinant produced in Baculovirus is a single glycosylated polypeptide chain containing 113amino acids (109-211 aa) and having a molecular mass of 12.8kDa.GDNF is fused to an 10 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
GDNF protein (0.25mg/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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Introduction
Glial cell-derived neurotrophic factor or GDNF is part of the GDNF group of ligands proteins. GDNF has a crucial part in numerous cell mechanisms such as neurite outgrowth, cell differentiation, cell survival and migration of cells. GDNF enhances neurons survival via GFRa receptors (mainly GFRa1). The mentioned neurons can die as a result from Parkinson's disease or ALS (amyotrophic lateral sclerosis). This protein takes part in the development of the spermatogenesis & kidney, also, it has a role in alcohol metabolism as ameliorating.
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Synonyms
Glial cell line-derived neurotrophic factor, hGDNF, Astrocyte-derived trophic factor, ATF, ATF1, ATF2, HFB1-GDNF, HSCR3.
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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
ADPMRGQRGK NRGCVLTAIH LNVTDLGLGY ETKEELIFRY CSGSCDAAET TYDKILKNLS RNRRLVSDKV GQACCRPIAF DDDLSFLDDN LVYHILRKHS AKRCGCIHHH HHH
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Background
What is the molecular weight/Mw of GDNF HUMAN, SF9 Protein?
GDNF HUMAN, SF9 Protein has a total Mw of 12.8kDa.
What is the source or expression system of GDNF HUMAN, SF9 Protein?
Sf9, Baculovirus cells.
What is the Purity of GDNF HUMAN, SF9 Protein?
GDNF HUMAN, SF9 Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of GDNF HUMAN, SF9 Protein?
The biological functionality of GDNF HUMAN, SF9 Protein will be determined in the future.
What is the amino acid sequence of GDNF HUMAN, SF9 Protein?
ADPMRGQRGK NRGCVLTAIH LNVTDLGLGY ETKEELIFRY CSGSCDAAET TYDKILKNLS RNRRLVSDKV GQACCRPIAF DDDLSFLDDN LVYHILRKHS AKRCGCIHHH HHH
What applications can GDNF HUMAN, SF9 Protein be used in?
GDNF HUMAN, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for GDNF HUMAN, SF9 Protein?
The endotoxin level is minimal, GDNF HUMAN, SF9 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 :
Lamin-A HumanDescription:
Lamin-A Human Recombinant
Prelamin-A/C, LMNA, LMN1, Lamin-A/C, 70 kDa lamin, Renal carcinoma antigen NY-REN-32, FPL, IDC, LFP, CDDC, EMD2, FPLD, HGPS, LDP1, LMNC, PRO1, CDCD1, CMD1A, FPLD2, LMNL1, CMT2B1, LGMD1B.
Product # :
PRO-690Price :
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Description
Recombinant Human Lamin A produced in E.Coli is a single, non-glycosylated polypeptide chain containing 645 amino acids and having a molecular mass of 70 kDa. Lamin-A protein is fused to a 6xHis tag at N-terminus and purified by conventional chromatography techniques.
Source
Escherichia Coli.
Formulation
The Lamin-A Protein solution (0.9mg/ml) contains 20mM phosphate buffer pH 7.0, 500mM NaCl, 1mM DTT, 1.5mM EDTA and 20% (v/v) Glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Lamin-A is a major component of the nuclear lamina, a dynamic meshwork located just under the nuclear envelope and it is encoded by lamin A/C gene (LMNA).
Lamin-A is synthesized as Prelamin A, a longer precursor that in vivo goes through a serial post-translational modifications that lead to mature Lamin A.
Diverse mutations in the Lamin A/C gene are associated with different diseases that are collectively called laminophaties, including Emery-Dreifuss muscular dystrophy, familiar partial lipodystrophy, limb girdle muscular dystrophy, dilated cardiomyopathy, Charcot-Marie-Tooth disease, and Hutchinson-Gilford progeria syndrome. -
Synonyms
Prelamin-A/C, LMNA, LMN1, Lamin-A/C, 70 kDa lamin, Renal carcinoma antigen NY-REN-32, FPL, IDC, LFP, CDDC, EMD2, FPLD, HGPS, LDP1, LMNC, PRO1, CDCD1, CMD1A, FPLD2, LMNL1, CMT2B1, LGMD1B.
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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. Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
HHHHHH-METPSQRRATRSGAQASSTPLSPTRITRLQEKEDLQELNDRLAVYIDRVHSLETENAGLRLRITES
EEVVSREVSGIKAAYEAELGDARKTLDSVAKERARLQLELSKVREEFKELKARNTKKEGDLIAAQA
RLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRL
QTMKEELDFQKNIYSEELRETKRRHETRLVEIDNGKQREFESRLADALQELRAQHEDQVEQYKKE
LEKTYSAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLA
RERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEERLRLSPSP
TSQRSRGRASSHSSQTQGGGSVTKKRKLESTESRSSFSQHARTSGRVAVEEVDEEGKFVRLRN
KSNEDQSMGNWQIKRQNGDDPLLTYRFPPKFTLKAGQVVTIWAAGAGATHSPPTDLVWKAQNT
WGCGNSLRTALINSTGEEVAMRKLVRSVTVVEDDEDEDGDDLLHHHHGSHCSSSGDPAEYNLRS
RTVLCGTCGQPADKASASGSGAQVGGPISSGSSASSVTVTRSYRSVGGSGGGSFGDNLVTRS
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 :
Leptin PAT7E10AT AntibodyDescription:
Leptin Clone PAT7E10AT, Mouse Anti Human
OB Protein, Obesity Protein, OBS, Obesity factor.
Product # :
ANT-690Price :
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Shipped with Ice Packs
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- More Info
Formulation
1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.
More Info
-
Introduction
A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.
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Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
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Physical Appearance
Sterile filtered colorless solution.
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Immunogen
Anti-human Leptin mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human Leptin amino acids 22-167 purified from E. coli.
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Ig Subclass
Mouse IgG2b heavy chain and k light chain.
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Clone
PAT7E10AT.
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Applications
Leptin antibody has been tested by ELISA, Western blot analysis and ICC/IF to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.
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Type
Mouse Anti Human Monoclonal.
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Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
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Purification Method
Leptin antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.
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 :
MICA Human, HisDescription:
MHC class I chain-related gene A, Human Recombinant His Tag
MHC class I polypeptide-related sequence A, MIC-A, MICA, PERB11.1, HLA-B, AS, HLAB, HLAC, SPDA1, HLA-B73, HLA-B-7301.
Product # :
PRO-2207Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
MICA Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 283 amino acids (24-297aa) and having a molecular mass of 32.7kDa.MICA is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MICA protein solution (0.25mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
MICA (MHC class I chain-related gene A) is a transmembrane glycoprotein that functions as a ligand for human NKG2D. A closely related protein, MICB, shares 85% amino acid identity with MICA. These proteins are distantly related to the MHC class I proteins. They possess three extracellular Ig-like domains, but they have no capacity to bind peptide or interact with ?2-microglobulin. The genes encoding these proteins are found within the Major Histocompatibility Complex on human chromosome 6. The MICA locus is highly polymorphic with more than 50 recognized human alleles. MICA is absent from most cells but is frequently expressed in epithelial tumors and can be induced by bacterial and viral infections. MICA is a ligand for human NKG2D, an activating receptor expressed on NK cells, NKT cells,gammadelta T cells, and CD8+beta T cells. Recognition of MICA by NKG2D results in the activation of cytolytic activity and/or cytokine production by these effector cells. MICA recognition is involved in tumor surveillance, viral infections, and autoimmune diseases.
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Synonyms
MHC class I polypeptide-related sequence A, MIC-A, MICA, PERB11.1, HLA-B, AS, HLAB, HLAC, SPDA1, HLA-B73, HLA-B-7301.
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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
MEPHSLRYNL TVLSWDGSVQ SGFLTEVHLD GQPFLRCDRQ KCRAKPQGQW AEDVLGNKTW DRETRDLTGN GKDLRMTLAH IKDQKEGLHS LQEIRVCEIH EDNSTRSSQH FYYDGELFLS QNLETEEWTM PQSSRAQTLA MNVRNFLKED AMKTKTHYHA MHADCLQELR RYLKSGVVLR RTVPPMVNVT RSEASEGNIT VTCRASGFYP WNITLSWRQD GVSLSHDTQQ WGDVLPDGNG TYQTWVATRI CQGEEQRFTC YMEHSGNHST HPVPSLEHHH HHH.
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 :
CST6 Human, ActiveDescription:
Cystatin E/M, BioActive Human Recombinant
Cystatin E/M, cystatin 6, Cystatin M, Cystatin-E, Cysteine proteinase inhibitor.
Product # :
PRO-2633Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CST6 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 142 amino acids (29-149 a.a.) and having a molecular mass of 15.9kDa.CST6 is fused to a 21 amino acid His tag at N-Terminus and purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The CST6 solution (0.5mg/1ml) contains 10% glycerol, 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
The IC50 value is < 10nM. The inhibitory function of Cystatin 6 on protease activity of papain was measured by a fluorometric assay using Z-FR-AMC at pH 7.5 at 25˚C.
More Info
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Introduction
Cystatin E/M or CST6 is part of the cystatin type 2 family. Part of the cystatin type 2 family members can act as cysteine protease inhibitors, whereas cystatin E/M regulates cathepsin B inhibitors and not cathepsin C. cystatin E/M is a protein the when secreted, has an effect on osteogenesis and bone resorption, insulin regulation, response to systemic inflammation & hepatocyte growth factor receptors.
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Synonyms
Cystatin E/M, cystatin 6, Cystatin M, Cystatin-E, Cysteine proteinase inhibitor.
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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 MRPQERMVGE LRDLSPDDPQ VQKAAQAAVA SYNMGSNSIY YFRDTHIIKA QSQLVAGIKY FLTMEMGSTD CRKTRVTGDH VDLTTCPLAA GAQQEKLRCD FEVLVVPWQN SSQLLKHNCV QM
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 :
CTHRC1 Human, HEKDescription:
Collagen Triple Helix Repeat Containing 1 Human Recombinant, HEK
Collagen Triple Helix Repeat Containing 1, Protein NMTC1, CTHRC1.
Product # :
PRO-2028Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
CTHRC1 Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (Ser31-Lys243) containing a total of 219 amino acids, having a calculated molecular mass of 23.9kDa and fused to a 6 aa His tag at C-Terminus.
Source
HEK 293.
Formulation
CTHRC1 was filtered (0.4µm) and lyophilized in phosphate buffered saline pH 7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Collagen triple helix repeat-containing protein 1 (CTHRC1) functions as a negative regulator of collagen matrix deposition. CTHRC1 is a secreted 28kDa protein which is glycosylated and highly conserved from lower chordates to mammals. CTHRC1 is highly connected with calcified tissues and cartilaginous matrix, but not with endothelial cells. CTHRC1 is detected qualitatively in plasma of healthy human subjects. CTHRC1 plasma levels are also significantly elevated during pregnancy, in diabetes, in inflammatory and infectious conditions, in subjects with acute myeloid leukemia but not in subjects with solid cancers. The hormonal functions of CTHRC1 include regulation of lipid storage and cellular glycogen levels with potentially far-reaching implications for cell metabolism and physiology. CTHRC1 gene deletion leads to fatty liver (steatosis) formation in mice while others exhibited inactivation of the CTHRC1 gene also results in low bone mass.
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Synonyms
Collagen Triple Helix Repeat Containing 1, Protein NMTC1, CTHRC1.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. CTHRC1 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
SEIPKGKQKA QLRQREVVDL YNGMCLQGPA GVPGRDGSPG ANGIPGTPGI PGRDGFKGEK GECLRESFEE SWTPNYKQCS WSSLNYGIDL GKIAECTFTK MRSNSALRVL FSGSLRLKCR NACCQRWYFT FNGAECSGPL PIEAIIYLDQ GSPEMNSTIN IHRTSSVEGL CEGIGAGLVD VAIWVGTCSD YPKGDASTGW NSVSRIIIEE LPK HHHHHH.
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 :
HERPUD1 HumanDescription:
HERPUD1 Human Recombinant
Homocysteine-responsive endoplasmic reticulum-resident ubiquitin-like domain member 1 protein, HERPUD1, Methyl methanesulfonate (MMF)-inducible fragment protein 1, HERP, KIAA0025, MIF1, Mif1, SUP.
Product # :
PRO-2105Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
HERPUD1 Human Recombinant produced in E. coli is a single polypeptide chain containing 286 amino acids (1-263) and having a molecular mass of 31.6kDa.HERPUD1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The HERPUD1 solution (0.5mg/1ml) contains Phosphate buffer saline (pH 7.4) and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
HERPUD1 is a multi-pass membrane protein which is a part of the endoplasmic reticulum quality control system. HERPUD1 owns 1 N-terminal ubiquitin-like domain and is expressed highly in the brain. HERPUD1 is also known as ER-associated degradation (ERAD) which takes part in ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins.
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Synonyms
Homocysteine-responsive endoplasmic reticulum-resident ubiquitin-like domain member 1 protein, HERPUD1, Methyl methanesulfonate (MMF)-inducible fragment protein 1, HERP, KIAA0025, MIF1, Mif1, SUP.
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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 MGSMESETEP EPVTLLVKSP NQRHRDLELS GDRGWSVGHL KAHLSRVYPE RPRPEDQRLI YSGKLLLDHQ CLRDLLPKQE KRHVLHLVCN VKSPSKMPEI NAKVAESTEE PAGSNRGQYP EDSSSDGLRQ REVLRNLSSP GWENISRPEA AQQAFQGLGP GFSGYTPYGW LQLSWFQQIY ARQYYMQYLA ATAASGAFVP PPSAQEIPVV SAPAPAPIHN QFPAENQPAN QNAAPQVVVN PGANQNLRMN AQGGPIVEED DEINRD.
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 :
SCGB1D1 HumanDescription:
Secretoglobin Family 1D, Member 1 Human Recombinant
Secretoglobin family 1D member 1, Lipophilin-A, SCGB1D1, LIPHA, LPNA, LIPA, LPHA.
Product # :
PRO-1602Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
SCGB1D1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 22-90) containing 79 amino acids including a 10 a.a N-terminal His tag. The total molecular mass is 8.8kDa (calculated).
Source
Escherichia Coli.
Formulation
SCGB1D1 filtered (0.4 µm) and lyophilized from 0.5mg/ml in 20mM Tris buffer and 50mM NaCl, pH 7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Secretoglobin Family 1D, Member 1 (SCGB1D1) belongs to the lipophilin subfamily, part of the uteroglobin superfamily, and is an ortholog of prostatein (which is the major secretory glycoprotein of the rat ventral prostate gland). SCGB1D1 binds androgens and other steroids. In addition SCGB1D1 binds chemotherapeutic drugs during the prostate cancer treatment. Steroid hormones regulate the SCGB1D1 transcription. SCGB1D1 is secreted into extracellular space. SCGB1D1 gene product represents one component of a heterodimeric molecule found in human tears whose elution profile is consistent with prostatein (which is a tetrameric molecule comprised of 3 peptide components in heterodimers).
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Synonyms
Secretoglobin family 1D member 1, Lipophilin-A, SCGB1D1, LIPHA, LPNA, LIPA, LPHA.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. SCGB1D1 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 VVCQALGSEI TGFLLAGKPV FKFQLAKFKA PLEAVAAKME VKKCVDTMAY EKRVLITKTL GKIAEKCDR.
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 :
SCGN HumanDescription:
Secretagogin Human Recombinant
SCGN, EF-hand calcium binding protein, Setagin, SEGN, CALBL, SECRET, DJ501N12.8, Secretagogin.
Product # :
PRO-599Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SCGN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 296 amino acids (1-276 a.a.) and having a molecular mass of 34.2kDa. SCGN is fused to a 20 amino acid His tag at N-terminus and purified by standard chromatography techniques.
Source
Escherichia Coli.
Formulation
SCGN His-Tag (1mg/ml) protein is supplied in 20mM Tris HCl pH-8, 1mM DTT, 0.1M NaCl and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
SCGN is a secreted calcium-binding protein which is found in the cytoplasm. It is related to calbindin D-28K and calretinin. Secretagogin is involved in KCL-stimulated calcium flux and cell proliferation.
Secretagogin plays a role in human non-functional pituitary adenomas. -
Synonyms
SCGN, EF-hand calcium binding protein, Setagin, SEGN, CALBL, SECRET, DJ501N12.8, Secretagogin.
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Physical Appearance
Sterile Filtered colorless liquid formulation.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MDSSREPTLG RLDAAGFWQV WQRFDADEKG YIEEKELDAF FLHMLMKLGT DDTVMKANLH KVKQQFMTTQ DASKDGRIRM KELAGMFLSE DENFLLLFRR ENPLDSSVEF MQIWRKYDAD SSGFISAAEL RNFLRDLFLH HKKAISEAKL EEYTGTMMKI FDRNKDGRLD LNDLARILAL QENFLLQFKM DACSTEERKR DFEKIFAYYD VSKTGALEGP EVDGFVKDMM ELVQPSISGV DLDKFREILL RHCDVNKDGK IQKSELALCL GLKINP.
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.