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Search results

1000 results found for “cellular retinoic acid binding protein”

Name

Description

Product #

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  • View Data Sheet

    Name :

    C-JUN Human (241 a.a.)

    Description:

    Jun Proto-Oncogene (1-241 a.a.) Human Recombinant

    Transcription factor AP-1, Activator protein 1, AP1, Proto-oncogene c-jun, V-jun avian sarcoma virus 17 oncogene homolog, p39, c-Jun.

    Product # :

    PKA-001

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    Description

    C-JUN 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 261 amino acids (1-241 a.a.) and having a molecular mass of 27.3kDa. The C-JUN is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The C-JUN solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol, 2mM DTT and 0.1M NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      C-JUN is a gene which, in combination with c-Fos, forms the AP-1early response transcription factor. C-JUN is activated by the JNKpathway. C-JUN is the putative transforming gene of avian sarcoma virus 17. C-JUN is a protein which is highly similar to the viral protein, and which interacts directly with specific target DNA sequences to regulate gene expression. The C-JUN gene is intronless and is mapped to 1p32-p31, a chromosomal region involved in both translocations and deletions in human malignancies.

    • Synonyms

      Transcription factor AP-1, Activator protein 1, AP1, Proto-oncogene c-jun, V-jun avian sarcoma virus 17 oncogene homolog, p39, c-Jun.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MTAKMETTFY DDALNASFLP SESGPYGYSN PKILKQSMTL NLADPVGSLK PHLRAKNSDL LTSPDVGLLK LASPELERLI IQSSNGHITT TPTPTQFLCP KNVTDEQEGF AEGFVRALAE LHSQNTLPSV TSAAQPVNGA GMVAPAVASV AGGSGSGGFS ASLHSEPPVY ANLSNFNPGA LSSGGGAPSY GAAGLAFPAQ PQQQQQPPHH LPQQMPVQHP RLQALKEEPQ TVPEMPGETP P.

    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.

    Cjun Human
  • View Data Sheet

    Name :

    CRYM Human

    Description:

    Crystallin, Mu Human Recombinant

    Crystallin Mu, Thiomorpholine-Carboxylate Dehydrogenase, THBP, NADP-Regulated Thyroid-Hormone Binding Protein, NADP-Regulated Thyroid-Hormone-Binding Protein, Mu-Crystallin Homolog, EC 1.5.1.25, DFNA40, CRYM.

    Product # :

    PRO-2291

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    Description

    CRYM Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 334 amino acids (1-314) and having a molecular mass of 35.9kDa. CRYM is fused to 20 a.a. His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CYRM 1mg/ml solution containing 20mM Tris-HCl buffer (pH8.0), 1mM DTT, and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Crystallin, Mu (CRYM) is a taxon-specific crystallin protein which binds NADPH and has sequence similarity to bacterial ornithine cyclodeaminases. CRYM doesn’t perform a structural role in lens tissue; instead CRYM binds thyroid hormone for possible regulatory or developmental roles. CRYM gene mutations are linked with autosomal dominant non-syndromic deafness. CRYM specifically catalyzes the reduction of imine bonds in brain substrates which may include cystathionine ketamine and lanthionine ketamine.

    • Synonyms

      Crystallin Mu, Thiomorpholine-Carboxylate Dehydrogenase, THBP, NADP-Regulated Thyroid-Hormone Binding Protein, NADP-Regulated Thyroid-Hormone-Binding Protein, Mu-Crystallin Homolog, EC 1.5.1.25, DFNA40, CRYM.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      CRYM although stable at 4°C for 1 week, should be stored 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.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MSRVPAFLSA AEVEEHLRSS SLLIPPLETA LANFSSGPEG GVMQPVRTVV PVTKHRGYLG VMPAYSAAED ALTTKLVTFY EDRGITSVVP SHQATVLLFE PSNGTLLAVM DGNVITAKRT AAVSAIATKF LKPPSSEVLC ILGAGVQAYS HYEIFTEQFS FKEVRIWNRT KENAEKFADT VQGEVRVCSS VQEAVAGADV IITVTLATEP ILFGEWVKPG AHINAVGASR PDWRELDDEL MKEAVLYVDS QEAALKESGD VLLSGAEIFA ELGEVIKGVK PAHCEKTTVF KSLGMAVEDT VAAKLIYDSW SSGK

    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.

    Crym Human
  • View Data Sheet

    Name :

    RNF181 Human

    Description:

    Ring Finger Protein 181 Human Recombinant

    Ring Finger Protein 181, E3 Ubiquitin-Protein Ligase RNF181, HSPC238, EC 6.3.2.-.

    Product # :

    PRO-1218

    Price :

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    Description

    RNF181 Human Recombinant produced in E. coli is a single polypeptide chain containing 176 amino acids (1-153) and having a molecular mass of 20.3 kDa.RNF181 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The RNF181 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      E3 ubiquitin-protein ligase RNF181 (RNF181) accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the thioester form and subsequently directly transfers the ubiquitin to targeted substrates. RNF181 is widely expressed, with the highest levels in the liver and heart and the lowest levels in the brain and skeletal muscle. RNF181 is also expressed in platelets (at protein level).

    • Synonyms

      Ring Finger Protein 181, E3 Ubiquitin-Protein Ligase RNF181, HSPC238, EC 6.3.2.-.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMASYFDE HDCEPSDPEQ ETRTNMLLEL ARSLFNRMDF EDLGLVVDWD HHLPPPAAKT VVENLPRTVI RGSQAELKCP VCLLEFEEEE TAIEMPCHHL FHSSCILPWL SKTNSCPLCR YELPTDDDTY EEHRRDKARK QQQQHRLENL HGAMYT.

    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.

    Rnf181 Human
  • View Data Sheet

    Name :

    RBM11 Human

    Description:

    RNA Binding Motif Protein 11 Human Recombinant

    Splicing regulator RBM11, RNA-binding motif protein 11, RBM11.

    Product # :

    PRO-1802

    Price :

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    Description

    RBM11 Human Recombinant produced in E. coli is a single polypeptide chain containing 304 amino acids (1-281) and having a molecular mass of 34.6kDa. RBM11 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The RBM11 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      RNA Binding Motif Protein 11 (RBM11) which contains 1 RNA recognition motif is a part of the RBM family. The RBM gene family encodes proteins with an RNA binding motif which participate in the modulation of apoptosis. RBM11 is expressed in testis, kidney, spleen, brain, spinal cord and mammary gland and can be found as 2 isoforms produced by alternative splicing.

    • Synonyms

      Splicing regulator RBM11, RNA-binding motif protein 11, RBM11.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMFPAQEE ADRTVFVGNL EARVREEILY ELFLQAGPLT KVTICKDREG KPKSFGFVCF KHPESVSYAI ALLNGIRLYG RPINVQYRFG SSRSSEPANQ SFESCVKINS HNYRNEEMLV GRSSFPMQYF PINNTSLPQE YFLFQKMQWH VYNPVLQLPY YEMTAPLPNS ASVSSSLNHV PDLEAGPSSY KWTHQQPSDS DLYQMTAPLP NSASVSSSLN HVPDLEAGPS SYKWTHQQPS DSDLYQMNKR KRQKQTSDSD SSTDNNRGNE CSQKFRKSKK KKRY.

    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.

    Rbm11 Human
  • View Data Sheet

    Name :

    Omentin 298 a.a. Human

    Description:

    Omentin 298 a.a. Human Recombinant

    Intelectin-1, HL1, LFR, HL-1, INTL, ITLN, hIntL.

    Product # :

    CYT-061

    Price :

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    Description

    Omentin Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 298 amino acids (17-313) and having a molecular mass of 33.2 kDa.The Omentin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Omentin protein (1mg/ml) is supplied in 20mM Tris-HCL, pH-8, 0.4M Urea and 10% Glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Omentin is a recently recognized gene highly localized to the mental tissue (visceral adipose tissue). Omentin is present in the stromal vascular cells in the adipose tissue rather than in the adipocytes. Omentin is predominantly expressed in the visceral adipose tissue than the subcutaneous tissue, with the omentin mRNA being 150 times higher in the visceral adipose tissue. Omentin has also been detected in human blood using western blot analysis, and seems to increase insulin-stimulated glucose uptake in 3T3-L1 adipocytes in mice. Omentin seems to increase Akt phosphorylation irrespective of insulin presence. Its role in glucose metabolism and obesity remains to be described; an insulin-sensitizing action is possible.Differences in Omentin expression has been noted in adipose tissue from normals and patients with inflammatory bowel disease although its significance is unknown.

    • Synonyms

      Intelectin-1, HL1, LFR, HL-1, INTL, ITLN, hIntL.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MWSTDEANTY FKEWTCSSSP SLPRSCKEIK DECPSAFDGL YFLRTENGVI YQTFCDMTSG GGGWTLVASV HENDMRGKCT VGDRWSSQQG SKAVYPEGDG NWANYNTFGS AEAATSDDYK NPGYYDIQAK DLGIWHVPNK SPMQHWRNSS LLRYRTDTGF LQTLGHNLFG IYQKYPVKYG EGKCWTDNGP VIPVVYDFGD AQKTASYYSP YGQREFTAGF VQFRVFNNER AANALCAGMR VTGCNTEHHC IGGGGYFPEA SPQQCGDFSG FDWSGYGTHV GYSSSREITE AAVLLFYR

    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.

    Omentin 298 Aa Human
  • View Data Sheet

    Name :

    GROEL (27-573) Human

    Description:

    GroEL (HSP60) (27-573 a.a.) Human Recombinant

    CPN60, GROEL, HLD4, HSP-60, HSP60, HSP65, HuCHA60, SPG13, Chaperonin 60, 60 kDa chaperonin, P60 lymphocyte protein, 60 kDa heat shock protein, mitochondrial.

    Product # :

    HSP-055

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    Description

    GROEL Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 572 amino acids (27-573 a.a.) and having a molecular mass of 60kDa.GROEL is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GROEL protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer, (pH 8.0) 0.1M NaCl and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      GroEL, HSP60 is a chaperonin located in the mitochondria which is responsible for the transportation & refolding of proteins from the cytoplasm directly into the mitochondrial matrix. GroEL is regulated by the HSP10 cochaperonin, which is a single heptameric protein ring having a molecular mass of 10 kDa which form a unique complex with HSP60. HSP10, GroES coordinates the ATPase activity of the HSP60 subunits in order to allow the release of bound polypeptide in a manner that is productive for its correct folding.

    • Synonyms

      CPN60, GROEL, HLD4, HSP-60, HSP60, HSP65, HuCHA60, SPG13, Chaperonin 60, 60 kDa chaperonin, P60 lymphocyte protein, 60 kDa heat shock protein, mitochondrial.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSHMAKDVK FGADARALML QGVDLLADAV AVTMGPKGRT VIIEQSWGSP KVTKDGVTVA KSIDLKDKYK NIGAKLVQDV ANNTNEEAGD GTTTATVLAR SIAKEGFEKI SKGANPVEIR RGVMLAVDAV IAELKKQSKP VTTPEEIAQV ATISANGDKE IGNIISDAMK KVGRKGVITV KDGKTLNDEL EIIEGMKFDR GYISPYFINT SKGQKCEFQD AYVLLSEKKI SSIQSIVPAL EIANAHRKPL VIIAEDVDGE ALSTLVLNRL KVGLQVVAVK APGFGDNRKN QLKDMAIATG GAVFGEEGLT LNLEDVQPHD LGKVGEVIVT KDDAMLLKGK GDKAQIEKRI QEIIEQLDVT TSEYEKEKLN ERLAKLSDGV AVLKVGGTSD VEVNEKKDRV TDALNATRAA VEEGIVLGGG CALLRCIPAL DSLTPANEDQ KIGIEIIKRT LKIPAMTIAK NAGVEGSLIV EKIMQSSSEV GYDAMAGDFV NMVEKGIIDP TKVVRTALLD AAGVASLLTT AEVVVTEIPK EEKDPGMGAM GGMGGGMGGG MF.

    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.

    Groel 27 573 Human
  • View Data Sheet

    Name :

    S100A1 Mouse

    Description:

    S100 Calcium Binding Protein A1 Mouse Recombinant

    Protein S100-A1, S-100 protein alpha chain, S-100 protein subunit alpha, S100 calcium-binding protein A1, S100a1, S100, S100a, AI266795.

    Product # :

    PRO-237

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    Description

    S100A1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 114 amino acids (1-94 a.a) and having a molecular mass of 12.6kDa (molecular weight on SDS-PAGE will appear higher).S100A1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    S100A1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 30% glycerol and 0.1M NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      S100A1 is a member of the S100 family of calcium binding proteins with EF-hand type Ca+2 binding motive. S100A1 (Calcium Binding Protein A1) is involved in the activation of sarcoplasmatic calcium release and the regulation of intermediate filament polymerization. S100A1 may function in stimulation of Ca2+-induced Ca2+ release, inhibition of microtubule assembly, and inhibition of protein kinase C-mediated phosphorylation. Reduced expression of S100A1 has been implicated in cardiomyopathies.
      S100 proteins are localized either in the cytoplasm or the nucleus of a wide range of cells. There are at least 13 members in the S100 gene family, which are located as a cluster on chromosome 1q21.

    • Synonyms

      Protein S100-A1, S-100 protein alpha chain, S-100 protein subunit alpha, S100 calcium-binding protein A1, S100a1, S100, S100a, AI266795.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSELESAME TLINVFHAHS GKEGDKYKLS KKELKDLLQT ELSGFLDVQK DADAVDKVMK ELDENGDGEV DFKEYVVLVA ALTVACNNFF WETS.

    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.

    S100A1 Mouse
  • View Data Sheet

    Name :

    Resistin Rat

    Description:

    Resistin Rat Recombinant

    Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, RSTN, XCP1, RETN1, MGC126603, MGC126609.

    Product # :

    CYT-1129

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    Description

    Resistin Rat Recombinant produced in E.Coli is disulfide-linked homodimer consisting of 2x95 amino acid polypeptide chains and having a molecular mass of approximately 20.2kDa.Resistin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2μm filtered concentrated solution in PBS, pH7.4 and 0.02 % Tween-20.

    Purity

    Greater than 97.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Resistin, a product of the RSTN gene, is a peptide hormone belongs to the class of cysteine-rich secreted proteins (monomeric peptide contains 11 cysteine residues) referred to as the RELM family, and is also described as ADSF (Adipose Tissue-Specific Secretory Factor) or FIZZ3 (Found in Inflammatory Zone 3). Resistin may be an important link between obesity. Mouse resistin, specifically produced and secreted by adipocyte, acts on skeletal muscle myocytes, hepatocytes and adipocytes themselves so that it reduces their sensitivity. Steppan et al. have suggested that resistin suppressed the ability to stimulate glucose uptake. They have also suggested that resistin was present at elevated levels in blood of obese mice, and was down regulated by fasting and by antidiabetic drugs. Way et al., on the other hand, have found that resistin expression is severely suppressed in obesity.
      Other studies have shown that mouse resistin increases during the differentiation of adipocytes, but it also seems to inhibit adipogenesis. In contrast, the human adipogenic differentiation is likely to be associated with a down regulation of resistin gene expression.

    • Synonyms

      Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, RSTN, XCP1, RETN1, MGC126603, MGC126609.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Resistin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Resistin should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Resistin in sterile PBS not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MPSMSLCPMD EAISKKINQD FSSLLPAAMK NTVLHCWSVS SRGRLASCPE GTTVTSCSCG SGCGSWDVRE DTMCHCQCGS IDWTAARCCT LRVGS.

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    Rat Resistin Protein
  • View Data Sheet

    Name :

    SDCBP Human

    Description:

    Syndecan Binding Protein Human Recombinant

    SYCL, syntenin-1, Syndecan-binding protein 1, Scaffold protein Pbp1, MDA-9, Melanoma differentiation-associated protein 9, TACIP18, Pro-TGF-alpha cytoplasmic domain-interacting protein 18.

    Product # :

    PRO-036

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    Description

    SDCBP produced in E.Coli is a single, non-glycosylated polypeptide chain containing 318 amino acids (1-298a.a.) and having a molecular mass of 34.6kDa.SDCBP is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SDCBP protein solution (0.5mg/1ml) is formulated in 20 mM Tris-HCl Buffer (pH 8.0), 100 mM NaCl, and 40% Glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      SDCBP is a multifunctional intracellular adapter protein. SDCBP protein has tandemly repeated PDZ domains which react with the FYA (phe-tyr-ala) carboxyterminal amino acid sequence of the syndecans. SDCBP is has a role in organization of protein complexes in the plasma membranes, regulation of B-cell development, activation of transcription factors, intracellular trafficking and cell-surface targeting, synaptic transmission, and axonal outgrowth.

    • Synonyms

      SYCL, syntenin-1, Syndecan-binding protein 1, Scaffold protein Pbp1, MDA-9, Melanoma differentiation-associated protein 9, TACIP18, Pro-TGF-alpha cytoplasmic domain-interacting protein 18.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.Please avoid freeze thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MSLYPSLEDL KVDKVIQAQT AFSANPANPA ILSEASAPIP HDGNLYPRLY PELSQYMGLS LNEEEIRANV AVVSGAPLQG QLVARPSSIN YMVAPVTGND VGIRRAEIKQ GIREVILCKD QDGKIGLRLK SIDNGIFVQL VQANSPASLV GLRFGDQVLQ INGENCAGWS SDKAHKVLKQ AFGEKITMTI RDRPFERTIT MHKDSTGHVG FIFKNGKITS IVKDSSAARN GLLTEHNICE INGQNVIGLK

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    Sdcbp Human
  • View Data Sheet

    Name :

    MAD2L1BP Human

    Description:

    MAD2L1 Binding Protein Human Recombinant

    MAD2L1-binding protein, Caught by MAD2 protein, MAD2L1BP, CMT2, KIAA0110, RP1-261G23.6.

    Product # :

    PRO-1052

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    Description

    MAD2L1BP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 298 amino acids (1-274 a.a) and having a molecular mass of 33.6kDa (Molecular weight on SDS-PAGE will appear higher).MAD2L1BP is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MAD2L1BP protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 100mM NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      MAD2L1-binding protein (MAD2L1BP) is a member of the MAD2L1BP family.MAD2L1BP is a binding protein of the MAD2 mitotic arrest deficient-like 1 (MAD2/MAD2L1). MAD2 is a fundamental factor of the spindle checkpoint which delays the onset of anaphase until all the kinetochores are connected to the spindle. The MAD2L1BP protein acts to curb the spindle checkpoint and allow mitosis to proceed through anaphase by binding MAD2L1 once it dissociated from the MAD2L1-CDC20 complex. For the duration of the cell cycle, MAD2L1BP levels increase and then remain constant until late mitosis after which they drop.

    • Synonyms

      MAD2L1-binding protein, Caught by MAD2 protein, MAD2L1BP, CMT2, KIAA0110, RP1-261G23.6.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSHMAAPEA EVLSSAAVPD LEWYEKSEET HASQIELLET SSTQEPLNAS EAFCPRDCMV PVVFPGPVSQ EGCCQFTCEL LKHIMYQRQQ LPLPYEQLKH FYRKPSPQAE EMLKKKPRAT TEVSSRKCQQ ALAELESVLS HLEDFFARTL VPRVLILLGG
      NALSPKEFYE LDLSLLAPYS VDQSLSTAAC LRRLFRAIFM ADAFSELQAP PLMGTVVMAQ GHRNCGEDWF RPKLNYRVPS RGHKLTVTLS CGRPSIRTTA WEDYIWFQAP VTFKGFRE.

    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.

    Mad2L1Bp Human
  • View Data Sheet

    Name :

    RCVRN Mouse

    Description:

    Recoverin Mouse Recombinant

    RCV1, Cancer-associated retinopathy protein, Protein CAR, RCVRN, Recoverin, S-modulin.

    Product # :

    PRO-2547

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    Description

    Recoverin Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 225 amino acids (1-202a.a.) and having a molecular mass of 25.8kDa. Recoverin Mouse is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein (1mg/ml) contains Phosphate Buffered Saline (pH 7.4), 10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • 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.

    • Synonyms

      RCV1, Cancer-associated retinopathy protein, Protein CAR, RCVRN, Recoverin, S-modulin.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMGNSKSG ALSKEILEEL QLNTKFTEEE LSAWYQSFLK ECPSGRITRQ EFESIYSKFF PDSDPKAYAQ HVFRSFDANS DGTLDFKEYV IALHMTTAGK PTQKLEWAFS LYDVDGNGTI SKNEVLEIVM AIFKMIKPED VKLLPDDENT PEKRAEKIWA FFGKKEDDKL TEEEFIEGTL ANKEILRLIQ FEPQKVKERI KEKKQ.

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    Recoverin Mouse
  • View Data Sheet

    Name :

    C4BPB Human

    Description:

    Complement Component 4 Binding Protein, Beta Human Recombinant

    C4b-binding protein beta chain, C4BPB, C4BP.

    Product # :

    PRO-1174

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    Description

    C4BPB Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 260 amino acids (18-252 a.a) and having a molecular mass of 29kDa.C4BPB is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    C4BPB protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0) and 10% glycerol and 0.15M NaCl.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Complement Component 4 Binding Protein, Beta (C4BPB) belongs to a superfamily of proteins composed primarily of tandemly arrayed short consensus repeats of approximately 60 amino acids. C4BPB has a regulatory role in the coagulation system also, mediated via the beta-chain binding of protein S, a vitamin K-dependent protein which functions as a cofactor of activated protein C. A single, unique beta-chain of the C4BPB assembles with 7 identical alpha-chains into the principal isoform of C4BPB, which is a multimeric protein that controls activation of the complement cascade via the classical pathway. C4BPB binds as a cofactor to C3b/C4b inactivator (C3bINA), which subsequently hydrolyzes the complement fragment C4b. In addition, C4BPB accelerates the degradation of the C4bC2a complex (C3 convertase) by detaching the complement fragment C2a. Furthermore, C4BPB interacts with anticoagulant protein S and with serum amyloid P component.

    • Synonyms

      C4b-binding protein beta chain, C4BPB, C4BP.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSHMSDAEH CPELPPVDNS IFVAKEVEGQ ILGTYVCIKG YHLVGKKTLF CNASKEWDNT TTECRLGHCP DPVLVNGEFS SSGPVNVSDK ITFMCNDHYI LKGSNRSQCL EDHTWAPPFP ICKSRDCDPP GNPVHGYFEG NNFTLGSTIS YYCEDRYYLV GVQEQQCVDG EWSSALPVCK LIQEAPKPEC EKALLAFQES KNLCEAMENF MQQLKESGMT MEELKYSLEL KKAELKAKLL.

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    C4Bpb Human
  • View Data Sheet

    Name :

    VAMP3 Human

    Description:

    Synaptobrevin-3 Human Recombinant

    VAMP3, VAMP-3, Cellubrevin, Vesicle-Associated Membrane Protein 3, Synaptobrevin-3, CEB, SYB3.

    Product # :

    PRO-652

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    Description

    VAMP3 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.

    Source

    Escherichia Coli.

    Formulation

    The VAMP3 protein solution contains 20mM Tris pH-7.5 and 10% glycerol.

    Purity

    Greater than 95.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Citations

    More Info

    • Introduction

      VAMP3 is present in recycling endosomes and endosome-derived vesicles. VAMP3 has been implicated in recycling of transferrin receptors to the plasma membrane, secretion of alpha-granules in platelets, recycling of T-cell receptors to the immunological synapses, and membrane trafficking during cell migration. VAMP-3 is present in human platelets and necessary for granule secretion. Synaptobrevins are the main components of a protein complex involved in the docking and/or fusion of synaptic vesicles with the presynaptic membrane. VAMP3 high homology to other VAMPs in its broad tissue distribution and subcellular localization is shown to be the human equivalent of the rodent cellubrevin. In platelets the protein resides on a compartment that is not mobilized to the plasma membrane on calcium or thrombin stimulation.

    • Synonyms

      VAMP3, VAMP-3, Cellubrevin, Vesicle-Associated Membrane Protein 3, Synaptobrevin-3, CEB, SYB3.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MSTGPTAATG SNRRLQQTQN QVDEVVDIMR VNVDKVLERD QKLSELDDRA DALQAGASQF ETSAAKLKRK YWWKNCK.

    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.

    Vamp3 Human
  • View Data Sheet

    Name :

    EBAG9 Human

    Description:

    Estrogen Receptor Binding Site Associated Antigen 9 Human Recombinant

    EB9, PDAF, RCAS1, EBAG9, Receptor-binding cancer antigen expressed on SiSo cells, Cancer-associated surface antigen RCAS1, Estrogen receptor-binding fragment-associated gene 9 protein.

    Product # :

    PRO-343

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    Description

    EBAG9 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 207 amino acids (28-213) and having a molecular mass of 23.4 kDa. The EBAG9 protein is fused to a 20 amino acid His-Tag at N-terminus and purified by standard chromatography techniques.

    Source

    Escherichia Coli.

    Formulation

    The EBAG9 protein solution contains 20mM Tris-HCl pH-8, 1mM DTT, 2mM EDTA and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

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    • Introduction

      EBAG9 is a type III transmembrane protein that is primarily located in the Golgi. EBAG9 is a tumor-associated antigen that is expressed at high frequency in a variety of cancers, such as advanced breast and prostate cancers. while the EBAG9 acts to inhibit the growth of receptor-binding cells and induced apoptosis of immune cells, cancer cells may evade immune surveillance. Thus immunodetection of EBAG9 expression can be a negative prognostic indicator. EBAG9 promotes progression of bladder cancer. In rheumatoid arthritis, the deficiency of EBAG9 induces CTL infiltration through failure to evade immune attack, therefore leading to apoptosis of the synovial lining cells. EBAG9 is involved in controlling exocytosis processes. EBAG9 expression plays a role in the progression of oral squamous cell carcinoma. EBAG9 plays a specific role in premature stages of breast carcinogenesis.

    • Synonyms

      EB9, PDAF, RCAS1, EBAG9, Receptor-binding cancer antigen expressed on SiSo cells, Cancer-associated surface antigen RCAS1, Estrogen receptor-binding fragment-associated gene 9 protein.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MRSGRGRKLS GDQITLPTTV DYSSVPKQTD VEEWTSWDED APTSVKIEGG NGNVATQQNS LEQLEPDYFK DMTPTIRKTQ KIVIKKREPL NFGIPDGSTG FSSRLAATQD LPFIHQSSEL GDLDTWQENT NAWEEEEDAA WQAEEVLRQQ KLADREKRAA EQQRKKMEKE AQRLMKKEQN KIGVKLS.

    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.

    Ebag9 Human
  • View Data Sheet

    Name :

    ARPC5 Human

    Description:

    Actin Related Protein 2/3 Complex, Subunit 5 Human Recombinant

    Actin-related protein 2/3 complex subunit 5, Arp2/3 complex 16 kDa subunit, p16-ARC, ARPC5, ARC16, MGC88523, dJ127C7.3.

    Product # :

    PRO-145

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    Description

    ARPC5 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 171 amino acids (1-151 a.a.) and having a molecular mass of 18.4kDa. The ARPC5 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ARPC5 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 50% glycerol and 0.1M NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      ARPC5 is a 151 amino acid subunit of the Arp2/3 complex. ARPC5 is believed to have a role in maintaining the integrity of Arp2/3. ARPC5 is a substrate for MAPKAPK-2 which, via phosphorylation of ARPC5, may participate in Arp2/3 regulatory functions and remodeling of the Actin cytoskeleton.

    • Synonyms

      Actin-related protein 2/3 complex subunit 5, Arp2/3 complex 16 kDa subunit, p16-ARC, ARPC5, ARC16, MGC88523, dJ127C7.3.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MSKNTVSSAR FRKVDVDEYD ENKFVDEEDG GDGQAGPDEG EVDSCLRQGN MTAALQAALK NPPINTKSQA VKDRAGSIVL KVLISFKAND IEKAVQSLDK NGVDLLMKYI YKGFESPSDN SSAMLLQWHE KALAAGGVGS IVRVLTARKT V.

    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.

    Arpc5 Human
  • View Data Sheet

    Name :

    RBM3 Human

    Description:

    RNA Binding Motif Protein 3 Human Recombinant

    IS1-RNPL, RNPL, RNA-binding motif protein 3, Putative RNA-Binding Protein 3, RNA Binding Motif (RNP1, RRM) Protein 3.

    Product # :

    PRO-1462

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    Description

    RBM3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 180 amino acids (1-157 a.a) and having a molecular mass of 19kDa. RBM3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    RBM3 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol and 5mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      RBM3 belongs to the glycine-rich RNA-binding protein family and encodes a protein with one RNArecognition motif (RRM) domain. By cold shock and low oxygen tension the expression of this gene is induced. On chromosome 1 a pseudogene exists. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.Diseases associated with RBM3 include vaccinia, andcryptorchidism. GO annotations linked to this gene include RNA binding and ribosomal large subunit binding. An important paralog of this gene is RBMY1J.

    • Synonyms

      IS1-RNPL, RNPL, RNA-binding motif protein 3, Putative RNA-Binding Protein 3, RNA Binding Motif (RNP1, RRM) Protein 3.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMSSEEGK LFVGGLNFNT DEQALEDHFS SFGPISEVVV VKDRETQRSR GFGFITFTNP EHASVAMRAM NGESLDGRQI RVDHAGKSAR GTRGGGFGAH GRGRSYSRGG GDQGYGSGRY YDSRPGGYGY GYGRSRDYNG RNQGGYDRYS GGNYRDNYDN

    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.

    Rbm3 Human
  • View Data Sheet

    Name :

    SGTA Human

    Description:

    Small Glutamine-Rich Tetratricopeptide Repeat-Containing Protein Alpha Human Recombinant

    alphaSGT, hSGT, SGT, Vpu-binding protein, UBP, Small glutamine-rich tetratricopeptide repeat-containing protein alpha, Alpha-SGT, SGT1.

    Product # :

    PRO-807

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    Description

    SGTA Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 321 amino acids (1-313 a.a.) and having a molecular mass of 35.1 kDa. SGTA protein is fused to a 8 amino acid His-Tag at C-terminus and purified by standard chromatography.

    Source

    Escherichia Coli.

    Formulation

    SGTA Human solution containing 20mM Trsi HCL pH-8, 1mM DTT and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      SGTA is a ubiquitously expressed protein that contains three TPR protein-protein interaction duplicates. SGTA takes part as a component of the androgen receptor (AR)-chaperone-cochaperone complex, functions as a cochaperone and participates in androgen signaling. SGTA binds directly to HSC70 and HSP70 and mediates their ATPase activity. SGTA gene encodes a protein that is able to interact with the chief nonstructural protein of parvovirus H-1 and 70-kDa heat shock cognate. In addition, SGTA interacts with Vpu and Gag from HIV-1, SARS-CoV accessory protein 7a, DNAJC5 and DNAJC5B. Since this transcript is expressed universally in several tissues, SGTA serves a housekeeping function. While being involved in apoptosis and androgen signaling, SGTA is a possible molecule for polycystic ovary syndrome, a disorder characterized by androgen excess, obesity and menstrual disturbances.

    • Synonyms

      alphaSGT, hSGT, SGT, Vpu-binding protein, UBP, Small glutamine-rich tetratricopeptide repeat-containing protein alpha, Alpha-SGT, SGT1.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MDNKKRLAYA IIQFLHDQLR HGGLSSDAQE SLEVAIQCLE TAFGVTVEDS DLALPQTLPE IFEAAATGKE MPQDLRSPAR TPPSEEDSAE AERLKTEGNE QMKVENFEAA VHFYGKAIEL NPANAVYFCN RAAAYSKLGN YAGAVQDCER AICIDPAYSK AYGRMGLALS SLNKHVEAVA YYKKALELDP DNETYKSNLK IAELKLREAP SPTGGVGSFD IAGLLNNPGF MSMASNLMNN PQIQQLMSGM ISGGNNPLGT PGTSPSQNDL ASLIQAGQQF AQQMQQQNPE LIEQLRSQIR SRTPSASNDD QQELEHHHHH H.

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    Sgta Human
  • View Data Sheet

    Name :

    RELM b Human

    Description:

    RELM-Beta Human Recombinant

    Resistin-like beta, RELM beta, Cysteine-rich secreted protein FIZZ2, Colon and small intestine-specific cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 1, Colon carcinoma-related gene protein, RELM-b, XCP2, HXCP2.

    Product # :

    CYT-780

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    Description

    RELM-b Human Recombinant produced in E.Coli is a disulfide-linked homodimer, non-glycosylated, polypeptide chain containing 2 x 89 amino acids and having a total molecular mass of 19kDa. RELM-b is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    RELM-b was lyophilized from a solution containing 0.1% Trifluoroacetic Acid (TFA).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      RELM-beta (Resistin-Like Molecule-beta) is a member of a recently identified family of secreted proteins containing a conserved cystein-rich C-terminus. The RELM family consists of resistin (also called FIZZ3), RELM-alfa (FIZZ1), RELM-beta (FIZZ2) and RELM-gamma. Only resisistin and RELM-beta were found in humans whereas all four RELM family members were identified in rodents.
      RELM-beta appears to be produced as a homodimer exclusively by intestinal goblet cells and can be found in high quantities in stool. Remarkably, stool of germ-free mice displaying sterile intestinal tract does not contain RELM-beta until bacterial colonization takes place after pathogen-free mice entered natural environment. Some, but not all, colon carcinoma cell lines secrete RELM-beta into the cell culture supernatant.
      The physiological function of RELM-beta is not known. High doses of recombinant RELM-beta showed hyperglycemic effects including lowered glucose disposal and increased hepatic glucose production in mice.

    • Synonyms

      Resistin-like beta, RELM beta, Cysteine-rich secreted protein FIZZ2, Colon and small intestine-specific cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 1, Colon carcinoma-related gene protein, RELM-b, XCP2, HXCP2.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized RELM-b although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution RELM-b Human Recombinant should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized RELM-b in sterile 0.1% TFA not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MQCSLDSVMD KKIKDVLNSL EYSPSPISKK LSCASVKSQG RPSSCPAGMA VTGCACGYGC GSWDVQLETT CHCQCSVVDW TTARCCHLT.

    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.

    Relm B Human
  • View Data Sheet

    Name :

    YEATS4 Human

    Description:

    YEATS Domain Containing 4 Human Recombinant

    YEATS domain-containing protein 4, Glioma-amplified sequence 41, Gas41, NuMA-binding protein 1, NuBI-1, NuBI1, YEATS4, GAS41, YAF9, 4930573H17Rik, B230215M10Rik.

    Product # :

    PRO-1019

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    Description

    YEATS4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 250 amino acids (1-227 a.a.) and having a molecular mass of 28.9kDa. YEATS4 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    YEATS4 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 30% glycerol, 2mM DTT,0.2M NaCl and 0.1mM PMSF.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      YEATS Domain Containing 4 (YEATS4) has a high sequence homology to the human MLLT1, and yeast and human MLLT3 proteins. MLLT1 and MLLT3 proteins, both belong to a group of transcription factors, which indicates that YEATS might also represent a transcription factor. YEATS is believed to be necessary for RNA transcription. The YEATS gene has been shown to be amplified in tumors.

    • Synonyms

      YEATS domain-containing protein 4, Glioma-amplified sequence 41, Gas41, NuMA-binding protein 1, NuBI-1, NuBI1, YEATS4, GAS41, YAF9, 4930573H17Rik, B230215M10Rik.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMFKRMAE FGPDSGGRVK GVTIVKPIVY GNVARYFGKK REEDGHTHQW TVYVKPYRNE DMSAYVKKIQ FKLHESYGNP LRVVTKPPYE ITETGWGEFE IIIKIFFIDP NERPVTLYHL LKLFQSDTNA MLGKKTVVSE FYDEMIFQDP TAMMQQLLTT SRQLTLGAYK HETEFAELEV KTREKLEAAK KKTSFEIAEL KERLKASRET INCLKNEIRK LEEDDQAKDI.

    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.

    Yeats4 Human
  • View Data Sheet

    Name :

    SH3BGRL Human

    Description:

    SH3 Domain Binding Glutamic Acid-Rich Protein Like Human Recombinant

    SH3 domain-binding glutamic acid-rich-like protein, SH3BGRL, SH3BGR.

    Product # :

    PRO-1159

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    Description

    SH3BGRL Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 138 amino acids (1-114 a.a) and having a molecular mass of 15.3kDa.SH3BGRL is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SH3BGRL protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.15M NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      SH3 domain-binding glutamic acid-rich-like protein (SH3BGRL) belongs to the human SH3BGR family. SH3BGRL gene which is located to chromosome Xq13.3, encodes a small protein of 114 amino acids that is extensively expressed in various tissues including liver and blood. SH3BGRL protein contains a prolinerich sequence (PLPPQIF), which is comprsed of both the SH3 binding (PXXP)3 and the Homer EVH1 binding (PPXXF)4 motif.

    • Synonyms

      SH3 domain-binding glutamic acid-rich-like protein, SH3BGRL, SH3BGR.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSHMVIRVY IASSSGSTAI KKKQQDVLGF LEANKIGFEE KDIAANEENR KWMRENVPEN SRPATGYPLP PQIFNESQYR GDYDAFFEAR ENNAVYAFLG LTAPPGSKEA EVQAKQQA.

    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.

    Sh3Bgrl Human
  • View Data Sheet

    Name :

    RCHY1 Human

    Description:

    Ring Finger & CHY Zinc Finger Domain Containing 1 Human Recombinant

    ARNIP, CHIMP, hARNIP, PIRH2, PIRH2E, PIRH2F, PRO1996, RNF199, ZNF363, RING finger and CHY zinc finger domain-containing protein 1, Androgen receptor N-terminal-interacting protein, CH-rich-interacting match with PLAG1, E3 ubiquitin-protein ligase Pirh2, RING finger protein 199, Zinc finger protein 363, p53-induced RING-H2 protein, hPirh2, RCHY1.

    Product # :

    PRO-1536

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    Description

    RCHY1 Human Recombinant produced in E. coli is a single polypeptide chain containing 284 amino acids (1-261) and having a molecular mass of 32.5kDa. RCHY1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The RCHY1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Ring Finger & CHY Zinc Finger Domain Containing 1 (RCHY1) acts as an ubiquitin ligase. RCHY1 mediates E3-dependent ubiquitination and proteasomal degradation of target proteins which among them are TP53, HDAC1 and CDKN1B, consequently regulating their levels and cell cycle progression. RCHY1 is also increases AR transcription factor activity.

    • Synonyms

      ARNIP, CHIMP, hARNIP, PIRH2, PIRH2E, PIRH2F, PRO1996, RNF199, ZNF363, RING finger and CHY zinc finger domain-containing protein 1, Androgen receptor N-terminal-interacting protein, CH-rich-interacting match with PLAG1, E3 ubiquitin-protein ligase Pirh2, RING finger protein 199, Zinc finger protein 363, p53-induced RING-H2 protein, hPirh2, RCHY1.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMAATARE DGASGQERGQ RGCEHYDRGC LLKAPCCDKL YTCRLCHDNN EDHQLDRFKV KEVQCINCEK IQHAQQTCEE CSTLFGEYYC DICHLFDKDK KQYHCENCGI CRIGPKEDFF HCLKCNLCLA MNLQGRHKCI ENVSRQNCPI CLEDIHTSRV VAHVLPCGHL LHRTCYEEML KEGYRCPLCM HSALDMTRYW RQLDDEVAQT PMPSEYQNMT VDILCNDCNG RSTVQFHILG MKCKICESYN TAQAGGRRIS LDQQ.

    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.

    Rchy1 Human
  • View Data Sheet

    Name :

    S100A3 Mouse

    Description:

    S100 Calcium Binding Protein A3 Mouse Recombinant

    Protein S100-A3, Protein S-100E, S100 calcium-binding protein A3, S100a3, S100E.

    Product # :

    PRO-1166

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    Description

    S100A3 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 125 amino acids (1-101 a.a) and having a molecular mass of 14.3kDa.S100A3 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    S100A3 protein solution (1mg/ml) containing 20mM Tris-HCl buffer, pH8.0, 10% glycerol, 2mM DTT and 150mM NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      S100A3 is part of S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized in the cytoplasm/nucleus of a broad range of cells, and takes part in the regulation of several cellular processes such as cell cycle progression and differentiation. S100A3 has the largest number of cysteines of all S100 proteins. S100A3 has high affinity for Zinc, and is widely expressed in human hair cuticle.

    • Synonyms

      Protein S100-A3, Protein S-100E, S100 calcium-binding protein A3, S100a3, S100E.

    • Physical Appearance

      S100A3 is supplied as a sterile filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSHMTRPLE QAVAAIVCTF QEYAGRCGDK YKICQSELKE LLQKELPTWT PSEFRECDYN KFMSVLDTNK DCEVDFGEYV RSLASLCLYC HEYFKECPPE PPCPQ.

    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.

    S100A3 Mouse
  • View Data Sheet

    Name :

    ACVR1 Human

    Description:

    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-1140

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    • sds-page
    • Citations

    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

    ACVR1 Human sds-page - Product image 1

    Citations

    More Info

    • 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.

    • 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.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      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.

    Acvr1 Human
  • View Data Sheet

    Name :

    SH3BGRL3 Human

    Description:

    SH3 Domain Binding Glutamic Acid-Rich Protein Like 3 Human Recombinant

    SH3 Domain Binding Glutamic Acid-Rich Protein Like 3, SH3BGRL3-Like Protein, SH3 Domain-Binding Protein 1, SH3BP-1, TNF Inhibitory Protein, TIP-B1.

    Product # :

    PRO-1216

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info
    • Citations

    Description

    SH3BGRL3 Human Recombinant produced in E. coli is a single polypeptide chain containing 116 amino acids (1-93) and having a molecular mass of 12.8 kDa.SH3BGRL3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The SH3BGRL3 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      SH3 domain-binding glutamic acid-rich-like protein 3 (SH3BGRL3) which is located on chromosome 1p34.3-35, encodes for a small 93 amino acids protein. SH3BGRL3 is the newest member of thioredoxin super family, whose posttranslational altered form was recognized as TNF-alpha inhibitory protein. SH3BGRL3 may act as a regulator in all-trans retinoic acid-induced pathway and also as a modulator of glutaredoxin biological activity.

    • Synonyms

      SH3 Domain Binding Glutamic Acid-Rich Protein Like 3, SH3BGRL3-Like Protein, SH3 Domain-Binding Protein 1, SH3BP-1, TNF Inhibitory Protein, TIP-B1.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMSGLRVY STSVTGSREI KSQQSEVTRI LDGKRIQYQL VDISQDNALR DEMRALAGNP KATPPQIVNG DQYCGDYELF VEAVEQNTLQ EFLKLA

    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.

    Sh3Bgrl3 Human
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