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Search results

1000 results found for “Leptin”

Name

Description

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  • View Data Sheet

    Name :

    EED Human

    Description:

    Embryonic Ectoderm Development Human Recombinant

    Embryonic ectoderm development, HEED; WAIT1, Polycomb protein EED, hEED, WD protein associating with integrin cytoplasmic tails 1, EED.

    Product # :

    PRO-1503

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    • More Info

    Description

    EED Human Recombinant produced in E. coli is a single polypeptide chain containing 464 amino acids (1-441) and having a molecular mass of 52.6kDa. EED is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      EED is a part of the Polycomb-group family whose members form multimeric protein complexe that are involved in preserving the transcriptional repressive state of genes over successive cell generations. EED mediates repression of gene activity through histone deacetylation, and acts as a specific regulator of integrin function. EED protein interacts with enhancer of zeste 2, the cytoplasmic tail of integrin ?7, immunodeficiency virus type 1 (HIV-1) MA protein, and histone deacetylase proteins.

    • Synonyms

      Embryonic ectoderm development, HEED; WAIT1, Polycomb protein EED, hEED, WD protein associating with integrin cytoplasmic tails 1, EED.

    • 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 MGSMSEREVS TAPAGTDMPA AKKQKLSSDE NSNPDLSGDE NDDAVSIESG TNTERPDTPT NTPNAPGRKS WGKGKWKSKK CKYSFKCVNS LKEDHNQPLF GVQFNWHSKE GDPLVFATVG SNRVTLYECH SQGEIRLLQS YVDADADENF YTCAWTYDSN TSHPLLAVAG SRGIIRIINP ITMQCIKHYV GHGNAINELK FHPRDPNLLL SVSKDHALRL WNIQTDTLVA IFGGVEGHRD EVLSADYDLL GEKIMSCGMD HSLKLWRINS KRMMNAIKES YDYNPNKTNR PFISQKIHFP DFSTRDIHRN YVDCVRWLGD LILSKSCENA IVCWKPGKME DDIDKIKPSE SNVTILGRFD YSQCDIWYMR FSMDFWQKML ALGNQVGKLY VWDLEVEDPH KAKCTTLTHH KCGAAIRQTS FSRDSSILIA VCDDASIWRW DRLR.

    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.

    Eed Human
  • View Data Sheet

    Name :

    SOST Human, HEK

    Description:

    Sclerostin Human Recombinant, HEK

    Sclerostin, SOST, CDD, VBCH.

    Product # :

    PRO-2481

    Price :

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    Description

    SOST Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (a.a 24-213) containing 196 amino acids including a 6 a.a C-terminal His tag. The total molecular mass is 22.4kDa (calculated).

    Source

    HEK293 Cells.

    Formulation

    SOST filtered (0.4 µm) and lyophilized from 0.5mg/ml in PBS and 5 % (w/v) trehalose, pH 7.4.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Sclerostin (SOST) is a secreted glycoprotein with a C-terminal cysteine knot-like (CTCK) domain and sequence similarity to the DAN (differential screening-selected gene aberrative in neuroblastoma) family of bone morphogenetic protein (BMP) antagonists. Sclerostin functions as a negative regulator of bone growth, by inhibiting bone formation. SOST is widely expressed at low levels, with highest levels in the bone, cartilage, kidney, liver, bone marrow and primary osteoblasts differentiated for 21 days. SOST gene defects cause sclerosteosis and bone dysplasia.

    • Synonyms

      Sclerostin, SOST, CDD, VBCH.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • 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 one week at 4°C.

    • 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. SOST is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      QGWQAFKNDA TEIIPELGEY PEPPPELENN KTMNRAENGG RPPHHPFETK DVSEYSCREL HFTRYVTDGP CRSAKPVTEL VCSGQCGPAR LLPNAIGRGK WWRPSGPDFR CIPDRYRAQR VQLLCPGGEA PRARKVRLVA SCKCKRLTRF HNQSELKDFG TEAARPQKGR KPRPRARSAK ANQAELENAY 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.

    Sost Protein
  • View Data Sheet

    Name :

    C12ORF5 Human

    Description:

    Chromosome 12 Open Reading Frame 5 Human

    Fructose-2,6-bisphosphatase TIGAR, TP53-induced glycolysis and apoptosis regulator, TIGAR, C12orf5.

    Product # :

    PRO-1791

    Price :

    Quantity :

    Shipping Method :

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    • description
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    Description

    TIGAR Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 270 amino acids and having a molecular mass of 30.1kDa. The TIGAR is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TIGAR was Lyophilized from a 0.2 µm filtered concentrated solution in 20mM Tris-HCl, pH8.5, 150mM NaCl.

    Purity

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

    More Info

    • Introduction

      TIGAR is a p53-inducible enzyme which catalyzes the hydrolysis of fructose-2-6 bisphosphate (F-2-6-BP) to fructose-6-phosphate and inorganic phosphate. F-2-6-BP is an influential activator of 6-phosphofructose-1 kinase (the rate limiting enzyme of glycolysis). By lowering the intracellular level of F-2-6-BP, TIGAR expression leads to increased glucose processing through the pentose phosphate pathway, the main cellular source for NADPH.

    • Synonyms

      Fructose-2,6-bisphosphatase TIGAR, TP53-induced glycolysis and apoptosis regulator, TIGAR, C12orf5.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized TIGAR stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution TIGAR should be stored at 4C between 2-7 days and for future use below -18C. 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 TIGAR in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MARFALTVVR HGETRFNKEK IIQGQGVDEP LSETGFKQAA AAGIFLNNVK FTHAFSSDLM RTKQTMHGIL ERSKFCKDMT VKYDSRLRER KYGVVEGKAL SELRAMAKAA REECPVFTPP GGETLDQVKM RGIDFFEFLC QLILKEADQK EQFSQGSPSN CLETSLAEIF PLGKNHSSKV NSDSGIPGLA ASVLVVSHGA YMRSLFDYFL TDLKCSLPAT LSRSELMSVT PNTGMSLFII NFEEGREVKP TVQCICMNLQ DHLNGLTETR

    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.

    Tigar Human
  • View Data Sheet

    Name :

    PHB2 Human

    Description:

    Prohibitin 2 Human Recombinant

    BAP, Bap37, BCAP37, p22, PNAS-141, REA, Prohibitin-2, B-cell receptor-associated protein BAP37, D-prohibitin, Repressor of estrogen receptor activity, PHB2.

    Product # :

    PRO-1533

    Price :

    Quantity :

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    • description
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    • More Info

    Description

    PHB2 Human Recombinant produced in E. coli is a single polypeptide chain containing 322 amino acids (1-299) and having a molecular mass of 35.7kDa. PHB2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PHB2 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.

    More Info

    • Introduction

      Prohibitin 2, also known as PHB2, mediates transcriptional repression by nuclear hormone receptors via recruitment of histone deacetylases by similarity. PHB2 functions as an estrogen receptor (ER)-selective coregulator which potentiates the inhibitory activities of antiestrogens and represses the activity of estrogens. PHB2 which is involved in regulating mitochondrial respiration activity and in aging, competes with NCOA1 for modulation of ER transcriptional activity.

    • Synonyms

      BAP, Bap37, BCAP37, p22, PNAS-141, REA, Prohibitin-2, B-cell receptor-associated protein BAP37, D-prohibitin, Repressor of estrogen receptor activity, PHB2.

    • 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 MGSMAQNLKD LAGRLPAGPR GMGTALKLLL GAGAVAYGVR ESVFTVEGGH RAIFFNRIGG VQQDTILAEG LHFRIPWFQY PIIYDIRARP RKISSPTGSK DLQMVNISLR VLSRPNAQEL PSMYQRLGLD YEERVLPSIV NEVLKSVVAK FNASQLITQR AQVSLLIRRE LTERAKDFSL ILDDVAITEL SFSREYTAAV EAKQVAQQEA QRAQFLVEKA KQEQRQKIVQ AEGEAEAAKM LGEALSKNPG YIKLRKIRAA QNISKTIATS QNRIYLTADN LVLNLQDESF TRGSDSLIKG KK.

    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.

    Phb2 Human
  • View Data Sheet

    Name :

    LPL Human

    Description:

    Lipoprotein Lipase Human Recombinant

    Lipoprotein lipase, LPL, LIPD, HDLCQ11.

    Product # :

    ENZ-086

    Price :

    Quantity :

    Shipping Method :

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    More Info

    • description
    • source
    • formulation
    • More Info

    Description

    The Recombinant Human LPL produced in E.coli has a molecular mass of 51.61kDa containing 458 amino acid residues of the human LPL and fused to a 10 a.a. His tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

    LPL was filtered (0.4 µm) and lyophilized from 0.5 mg/ml in 50mM Acetate buffer, pH=4.

    More Info

    • Introduction

      LPL is a lipoprotein lipase, which is expressed in the heart, muscle, and adipose tissue. LPL acts as a homodimer, and has the dual functions of triglyceride hydrolase and ligand/bridging factor for receptor-mediated lipoprotein uptake. Type I hyperlipoproteinemia is a result of severe mutations which cause LPL deficiency, whereas less extreme mutations in LPL are linked to many disorders of lipoprotein metabolism. Lipoprotein lipase (LPL) is a fundamental enzyme in plasma triglyceride hydrolysis and is secreted by macrophages in the subendothelial space. LPL also promotes the development of atherosclerosis through facilitation of monocyte adhesion to endothelial cells, stimulation of tumor necrosis factor alpha (TNF) secretion and induction of vascular smooth muscle cell proliferation.

    • Synonyms

      Lipoprotein lipase, LPL, LIPD, HDLCQ11.

    • 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.

    • Solubility

      It is recommended to add 0.1M Acetate buffer pH4 to prepare a working stock solution of approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10µg/ml. In higher concentrations the solubility of this antigen is limited. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MKHHHHHHAS ADQRRDFIDI ESKFALRTPE DTAEDTCHLI PGVAESVATC HFNHSSKTFM VIHGWTVTGM YESWVPKLVA ADQRRDFIDI ESKFALRTPE DTAEDTCHLI PGVAESVATC HFNHSSKTFM VIHGWTVTGM YESWVPKLVA ALYKREPDSN VIVVDWLSRA QEHYPVSAGY TKLVGQDVAR FINWMEEEFN YPLDNVHLLG YSLGAHAAGI AGSLTNKKVN RITGLDPAGP NFEYAEAPSR LSPDDADFVD VLHTFTRGSP GRSIGIQKPV GHVDIYPNGG TFQPGCNIGE AIRVIAERGL GDVDQLVKCS HERSIHLFID SLLNEENPSK AYRCSSKEAF EKGLCLSCRK NRCNNLGYEI SKVRAKRSSK MYLKTRSQMP YKVFHYQVKI HFSGTESETH TNQAFEISLY GTVAESENIP FTLPEVSTNK TYSFLIYTEV DIGELLMLKL KWKSDSYFSW SDWWSSPGFA IQKIRVKAGE TQKKVIFCSR EKVSHLQKGK APAVFVKCHD KSLNKKSG.

    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.

    Lpl Human
  • View Data Sheet

    Name :

    LTBR Human

    Description:

    Lymphotoxin Beta Receptor Human Recombinant

    Lymphotoxin Beta Receptor (TNFR Superfamily, Member 3), TNFCR,Tumor Necrosis Factor Receptor 2-Related Protein,Tumor Necrosis Factor Receptor Type III, Tumor Necrosis Factor C Receptor,D12S370, TNFRSF3,TNFR3,Tumor Necrosis Factor Receptor Superfamily Member 3,Lymphotoxin-Beta Receptor,Lymphotoxin B Receptor, LT-BETA-R,TNF-R-III, TNFR2-RP, TNF-RIII,TNFR-III, TNFR-RP, CD18, LTBR.

    Product # :

    CYT-853

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    Description

    LTBR Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 224 amino acids (28-227 a.a) and having a molecular mass of 24.6kDa.LTBR is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    LTBR protein solution (0.5mg/ml) containing PBS buffer (pH7.4) 10% glycerol and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Lymphotoxin Beta Receptor, also known as LTBR takes part in signaling during the development of lymphoid and other organs, lipid metabolism, immune response, and programmed cell death. In addition, the activity of this receptor has been associated to carcinogenesis. Alternatively spliced transcript variants encoding multiple isoforms have been observed for LTBR.

    • Synonyms

      Lymphotoxin Beta Receptor (TNFR Superfamily, Member 3), TNFCR,Tumor Necrosis Factor Receptor 2-Related Protein,Tumor Necrosis Factor Receptor Type III, Tumor Necrosis Factor C Receptor,D12S370, TNFRSF3,TNFR3,Tumor Necrosis Factor Receptor Superfamily Member 3,Lymphotoxin-Beta Receptor,Lymphotoxin B Receptor, LT-BETA-R,TNF-R-III, TNFR2-RP, TNF-RIII,TNFR-III, TNFR-RP, CD18, LTBR.

    • 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 MGSMSQPQAV PPYASENQTC RDQEKEYYEP QHRICCSRCP PGTYVSAKCS RIRDTVCATC AENSYNEHWN YLTICQLCRP CDPVMGLEEI APCTSKRKTQ CRCQPGMFCA AWALECTHCE LLSDCPPGTE AELKDEVGKG NNHCVPCKAG HFQNTSSPSA RCQPHTRCEN QGLVEAAPGT AQSDTTCKNP LEPLPPEMSG TMLM

    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.

    Ltbr Human
  • View Data Sheet

    Name :

    GREM1 Human

    Description:

    GREM1 Human Recombinant

    Gremlin-1 isoform 1, CKTSF1B1, DAND2, DRM, GREMLIN, IHG-2, PIG2, GREM1, Cell proliferation-inducing gene 2 protein, Cysteine knot superfamily 1, BMP antagonist 1, DAN domain family member 2, Down-regulated in Mos-transformed cells protein, Increased in high glucose protein 2.

    Product # :

    PRO-1359

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    Description

    GREM1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 183 amino acids (25-184) and having a molecular mass of 20.7 kDa. GREM1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GREM1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      GREM1 belongs to the BMP (bone morphogenic protein) antagonist family. Like BMPs, BMP antagonists comprise cystine knots and usually form homo- and heterodimers. The CAN (cerberus and dan) subfamily of BMP antagonists, to which GREM1 belongs, is characterized by a C-terminal cystine knot with an eight-membered ring. The antagonistic effect of the secreted glycosylated protein is because of its direct binding to BMP proteins. As an antagonist of BMP, GREM1 takes a place in regulating organogenesis, body patterning, and tissue differentiation. In mouse, GREM1 has been shown to convey the sonic hedgehog (SHH) signal from the polarizing region to the apical ectodermal ridge during limb bud outgrowth. Alternatively merged transcript variants encoding different isoforms have been found for this gene.

    • Synonyms

      Gremlin-1 isoform 1, CKTSF1B1, DAND2, DRM, GREMLIN, IHG-2, PIG2, GREM1, Cell proliferation-inducing gene 2 protein, Cysteine knot superfamily 1, BMP antagonist 1, DAN domain family member 2, Down-regulated in Mos-transformed cells protein, Increased in high glucose protein 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 MGSKKKGSQG AIPPPDKAQH NDSEQTQSPQ QPGSRNRGRG QGRGTAMPGE EVLESSQEAL HVTERKYLKR DWCKTQPLKQ TIHEEGCNSR TIINRFCYGQ CNSFYIPRHI RKEEGSFQSC SFCKPKKFTT MMVTLNCPEL QPPTKKKRVT RVKQCRCISI DLD.

    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.

    Grem1 Human
  • View Data Sheet

    Name :

    Procalcitonin Rhesus

    Description:

    Procalcitonin Rhesus Recombinant

    Calcitonin.

    Product # :

    HOR-016

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    Description

    Procalcitonin Rhesus Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (Ala26-Asn140) containing 125 amino acids including a 10 aa His tag at N-terminus. The total calculated molecular mass is 14kDa.

    Source

    Escherichia Coli.

    Formulation

    Procalcitonin was filtered (0.4µm) and lyophilized from 0.5mg/ml solution in 20mM Tris buffer and 50mM NaCl, pH 7.5.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Procalcitonin is a peptide hormone mainly produced by the C cells of the thyroid and certain endocrine cells of the lung. Under normal expression conditions, procalcitonin is immediately cleaved into three specific fragments, an N terminal residue, calcitonin and katacalcin. Levels of unprocessed procalcitonin rise significantly after bacterial infection, trauma or shock.

    • Synonyms

      Calcitonin.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • 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.

    • 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. Procalcitonin is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MKHHHHHHASAPFRSALESS PDPATLSEEE ARLLLAALVQ DYVQMKASEL EQEQETEGSS LDSPRSKRCG NLSTCMLGTY TQDFNKFHTF PQTAIGVGAP GKKRDMSSDL ERNRRRYVSM PQDAN.

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    Procalcitonin Rhesus
  • View Data Sheet

    Name :

    BPC-157

    Description:

    BPC-157 Pentadecapeptide

    Product # :

    HOR-029

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    Description

    BPC-157 Synthetic is a single, non-glycosylated polypeptide chain containing 15 amino acids, having a molecular mass of 1419.55 Dalton and a Molecular formula of C62H98N16O22.

    Formulation

    The protein was lyophilized with no additives.

    Purity

    Greater than 97.0% as determined by analysis by RP-HPLC.

    More Info

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized BPC-157 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution bpc-157 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 BPC-157 in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      H-Gly-Glu-Pro-Pro-Pro-Gly-Lys-Pro-Ala-Asp-Asp-Ala-Gly-Leu-Val-OH

    • Background

      BPC-157, short for Body Protection Compound-157, is a synthetic peptide that has garnered significant attention in the field of regenerative medicine and sports science. This peptide, derived from a portion of the human gastric juice protein known as BPC, exhibits remarkable healing and tissue regeneration properties. BPC-157 has shown promise in various preclinical and clinical studies, demonstrating its potential for the treatment of a wide range of injuries and disorders.

      The research on BPC-157 encompasses investigations into its mechanisms of action, efficacy, safety, and potential therapeutic applications. Studies have elucidated the peptide's ability to enhance angiogenesis, promote collagen synthesis, modulate inflammatory responses, and protect against oxidative stress. These properties make BPC-157 an intriguing candidate for accelerating tissue healing, reducing inflammation, and improving overall recovery outcomes.

      Preclinical studies have revealed the beneficial effects of BPC-157 in several injury models. For instance, BPC-157 has demonstrated its potential in accelerating tendon and ligament healing, mitigating muscle damage, and promoting bone regeneration. These findings suggest that BPC-157 could be a valuable therapeutic tool in orthopedic medicine and sports-related injuries.

      Furthermore, BPC-157 has exhibited promising effects on gastrointestinal health. Studies have highlighted its ability to protect and heal the gut lining, reduce ulcer formation, and alleviate symptoms associated with inflammatory bowel disease. These observations open up avenues for BPC-157 as a potential treatment for gastrointestinal disorders.

      In addition to its regenerative properties, BPC-157 has shown potential in neurological and psychiatric conditions. Research has indicated its neuroprotective effects, with implications for the treatment of traumatic brain injury, stroke, and neurodegenerative disorders. Preliminary studies also suggest BPC-157's potential as an antidepressant and anxiolytic agent.

      Despite the promising findings, further research is needed to fully understand the mechanisms underlying BPC-157's actions and to assess its long-term safety and efficacy. Clinical trials are underway to explore its potential therapeutic applications in humans, including its use in tendon and ligament repair, inflammatory bowel disease, and neurodegenerative disorders.

      This comprehensive review aims to summarize the current state of research on BPC-157, providing an overview of its mechanisms of action and therapeutic potential. By examining relevant studies and findings, we aim to shed light on the diverse applications of BPC-157 and its implications for regenerative medicine, sports science, and various disease

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    Bpc 157
  • View Data Sheet

    Name :

    CST3 Protein, His

    Description:

    Cystatin-C Human Recombinant, His Tag

    Cystatin-C, Cystatin-3, Neuroendocrine basic polypeptide, Gamma-trace, Post-gamma-globulin, CST3, MGC117328.

    Product # :

    PRO-656

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    Description

    Cystatin-C Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 129 amino acids and having a molecular mass of 14.5 kDa. The protein contains an extra His tag at N-terminus. The Cystatin-C amino acid sequence is identical to UniProtKB/Swiss-Prot entry Q6FGW9 amino acids 28–146.The Cystatin-C is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Filtered (0.4µm) and lyophilized from 0.5mg/ml in 20mM Tris buffer and 50mM NaCl pH-7.5.

    Purity

    Greater than 95% as determined by SDS PAGE.

    More Info

    • Introduction

      Cystatins are a superfamily of cysteine proteinase inhibitors found in both plants and animals. They comprise a group of proteinase inhibitors, widely distributed in tissues and body fluids, and form tight complexes with cysteine proteases such as cathepsin B, H, L and S. Cystatin C, a secreted molecule of this family, is of interest from biochemical, medicine and evolutionary points of view. Cystatin C, with molecular weight of 13260 Da, is composed of 120 amino acids, lacks carbohydrate and has two disulfide bridges located near the carboxyl terminus. Cystatin C is increased in patients with malignant diseases, and is related to the insufficiency of renal function and appears to be a better marker than creatinine. On the other hand, low levels of cystatin C involve cause the breakdown of the elastic laminae and, subsequently, the atherosclerosis and abdominal aortic aneurysm.

    • Synonyms

      Cystatin-C, Cystatin-3, Neuroendocrine basic polypeptide, Gamma-trace, Post-gamma-globulin, CST3, MGC117328.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized protein at –20°C. Aliquot reconstituted protein to avoid repeated freezing/thawing cycles and store at –80°C for long term storage. 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.

    • Solubility

      Add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

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    Cystatin C Human Recombinant
  • View Data Sheet

    Name :

    SCGN Rat

    Description:

    Secretagogin Rat Recombinant

    SCGN, EF-hand calcium binding protein, Setagin, SEGN, CALBL, Secretagogin.

    Product # :

    PRO-657

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    Description

    Secretagogin Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 286 amino acids and having a molecular mass of 33.3 kDa. The Rat SCGN is fused to a 10 a.a. His tag at N-Terminus.The protein’s amino acids sequence is identical to UniProtKB/Swiss-Prot entry Q6R556.The Rat SCGN is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The sterile filtered concentrated protein solution was lyophilized with 20mM Tris & 50mM NaCl pH-7.5.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • 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, Secretagogin.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • 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.

    • Solubility

      Add deionized water to a working concentration of 0.5mg/ml and let the lyophilized pellet dissolve completely.

    • Amino Acid Sequence

      MKHHHHHHAS MDNAHRQTQA HLDAACFWQI WQRFDKDEKG YIKETELDAF FDDLLAKFGI EDTLMEENVQ KMKEQLMVGH DISKEGRILM KELASMFLSE DENFLLFFRL ETPLDNSVEF MQIWRKYDAD SSGFISAAEL SNFLRDLFLH HKKVISEAEL EEYTSTMMKI FDRNKDGRLD LNDLARILAL QENFLLQFKM DASSTEERKR DFEKIFAHYD VSKTGALEGP EVDGFVKDMM ELVQPSISGV DLDKFREILL RHCDVNKDGK IQKSELALCLGLKINP.

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    Scgn Rat
  • View Data Sheet

    Name :

    MYLPF Human

    Description:

    Myosin Light chain, Phosphorylatable, Fast Skeletal Muscle Human Recombinant

    Myosin regulatory light chain 2 skeletal muscle isoform, Fast skeletal myosin light chain 2, MLC2B, MYLPF, MRLC2, MYL11, HUMMLC2B.

    Product # :

    PRO-243

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    Description

    MYLPF produced in E.Coli is a single, non-glycosylated polypeptide chain containing 189 amino acids (1-169 a.a) and having a molecular mass of 21.2kDa.MYLPF is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MYLPF protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 100mM NaCl.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Myosin regulatory light chains, including MRCL3, MYLPF and MYL9, regulate contraction in smooth muscle and non-muscle cells via phosphorylation by MLCK (myosin light chain kinase). Phosphorylation of myosin regulatory light chains, catalyzed by MLCK in the presence of calcium and calmodulin, increases the actin-activated myosin ATPase activity, thus regulating the contractile activity. MYLPF is vital for fast and slow skeletal muscle development.

    • Synonyms

      Myosin regulatory light chain 2 skeletal muscle isoform, Fast skeletal myosin light chain 2, MLC2B, MYLPF, MRLC2, MYL11, HUMMLC2B.

    • 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 MAPKRAKRRT VEGGSSSVFS MFDQTQIQEF KEAFTVIDQN RDGIIDKEDL RDTFAAMGRL NVKNEELDAM MKEASGPINF TVFLTMFGEK LKGADPEDVI TGAFKVLDPE GKGTIKKKFL EELLTTQCDR FSQEEIKNMW AAFPPDVGGN VDYKNICYVI THGDAKDQE.

    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.

    Mylpf Human
  • View Data Sheet

    Name :

    ASCC1 Human

    Description:

    Activating Signal Cointegrator 1 Complex Subunit 1 Human Recombinant

    Activating signal cointegrator 1 complex subunit 1, ASC1p50, CGI-18, p50, ASC-1 complex subunit p50, Trip4 complex subunit p50, ASCC1.

    Product # :

    PRO-1682

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    Description

    ASCC1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 380 amino acids (1-357) and having a molecular mass of 43.6 kDa.ASCC1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ASCC1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      ASCC1 is a subunit of the triggering signal cointegrator 1 (ASC-1) complex which is a transcriptional coactivator. ASC-1 complex takes a vital part in gene transactivation using various transcription factors such as activating protein 1 (AP-1), nuclear factor kappa-B (NF-kB) and serum response factor (SRF). ASCC1 has an N-terminal KH-type RNA-binding motif, essential for AP-1 transactivation by the ASC-1 complex. Alterations in ASCC1 result in Barrett esophagus and esophageal adenocarcinoma.

    • Synonyms

      Activating signal cointegrator 1 complex subunit 1, ASC1p50, CGI-18, p50, ASC-1 complex subunit p50, Trip4 complex subunit p50, ASCC1.

    • 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 MGSMEVLRPQ LIRIDGRNYR KNPVQEQTYQ HEEDEEDFYQ GSMECADEPC DAYEVEQTPQ GFRSTLRAPS LLYKHIVGKR GDTRKKIEME TKTSISIPKP GQDGEIVITG QHRNGVISAR TRIDVLLDTF RRKQPFTHFL AFFLNEVEVQ EGFLRFQEEV LAKCSMDHGV DSSIFQNPKK LHLTIGMLVL LSEEEIQQTC EMLQQCKEEF INDISGGKPL EVEMAGIEYM NDDPGMVDVL YAKVHMKDGS NRLQELVDRV LERFQASGLI VKEWNSVKLH ATVMNTLFRK DPNAEGRYNL YTAEGKYIFK ERESFDGRNI LKLFENFYFG SLKLNSIHIS QRFTVDSFGN YASCGQIDFS.

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    Ascc1 Human
  • View Data Sheet

    Name :

    EFNB3 Human

    Description:

    Ephrin- B3 Human Recombinant

    Ephrin-B3, EPH-related receptor transmembrane ligand ELK-L3, EPH-related receptor tyrosine kinase ligand 8, LERK-8, EFNB3, EPLG8, LERK8, EFL6.

    Product # :

    PRO-1169

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    Description

    EFNB3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 224 amino acids (28-226 a.a) and having a molecular mass of 24.6kDa.EFNB3 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    EFNB3 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 2M urea.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Ephrin-B3 (EFNB3) which belongs to the ephrin gene family is essential in brain development as well as in its maintenance. EFNB3 binds to, and induces the collapse of, commissural axons/growth cones in vitro. EFNB3 loosely binds Eph receptors located on bordering cells, leading to contact-dependent bidirectional signaling into neighboring cells. The EPH and EPH-related receptors comprise the largest subfamily of receptor protein-tyrosine kinases and are implicated in mediating developmental events, mostly in the nervous system.

    • Synonyms

      Ephrin-B3, EPH-related receptor transmembrane ligand ELK-L3, EPH-related receptor tyrosine kinase ligand 8, LERK-8, EFNB3, EPLG8, LERK8, EFL6.

    • 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 MGSHMLSLEP VYWNSANKRF QAEGGYVLYP QIGDRLDLLC PRARPPGPHS SPNYEFYKLY LVGGAQGRRC EAPPAPNLLL TCDRPDLDLR FTIKFQEYSP NLWGHEFRSH HDYYIIATSD GTREGLESLQ GGVCLTRGMK VLLRVGQSPR GGAVPRKPVS EMPMERDRGA AHSLEPGKEN LPGDPTSNAT SRGAEGPLPP PSMP.

    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.

    Efnb3 Human
  • View Data Sheet

    Name :

    EG VEGF Mouse

    Description:

    Endocrine Gland Vascular Endothelial Growth Factor Mouse Recombinant

    PK1, Prokineticin 1, EG-VEGF, Prok1, Endocrine-gland-derived vascular endothelial growth factor.

    Product # :

    CYT-825

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    Description

    EG-VEGF Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 86 amino acids and having a molecular mass of 9.6kDa.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in PBS pH7.4 and 3% Trehalose.

    Purity

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

    More Info

    • Introduction

      Endocrine gland-derived vascular endothelial growth factor (EG-VEGF) induces proliferation, migration, and fenestration in capillary endothelial cells derived from endocrine glands. Its expression is induced by hypoxia and is restricted to the steroidogenic glands (ovary, testis, adrenal, and placenta). Its expression is often complementary to the expression of VEGF (MIM 192240), suggesting that these molecules function in a coordinated manner. EG-VEGF potently contracts gastrointestinal (gi) smooth muscle. Induces proliferation, migration and fenestration (the formation of membrane discontinuities) in capillary endothelial cells derived from endocrine glands. Has little or no effect on a variety of other endothelial and non-endothelial cell types.

    • Synonyms

      PK1, Prokineticin 1, EG-VEGF, Prok1, Endocrine-gland-derived vascular endothelial growth factor.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized EG-VEGF Human Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EG-VEGF 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 Endocrine Gland Vascular Endothelial Growth Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      AVITGACERD IQCGAGTCCA ISLWLRGLRL CTPLGREGEE CHPGSHKIPF LRKRQHHTCP CSPSLLCSRF PDGRYRCFRD LKNANF.

    • Background

      What is the molecular weight/Mw of EG-VEGF Protein?
      EG-VEGF Protein has a total Mw of 9.6kDa.

      What is the source or expression system of EG-VEGF Protein?
      Escherichia Coli.

      What is the Purity of EG-VEGF Protein?
      EG-VEGF Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of EG-VEGF Protein?
      The biological functionality of EG-VEGF Protein will be determined in the future.

      What is the amino acid sequence of EG-VEGF Protein?
      AVITGACERD IQCGAGTCCA ISLWLRGLRL CTPLGREGEE CHPGSHKIPF LRKRQHHTCP CSPSLLCSRF PDGRYRCFRD LKNANF.

      What applications can EG-VEGF Protein be used in?
      EG-VEGF Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for EG-VEGF Protein?
      The endotoxin level is minimal, EG-VEGF 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.

    Eg Vegf Mouse
  • View Data Sheet

    Name :

    OPTC Human

    Description:

    Opticin Human Recombinant

    Opticin, Oculoglycan, OPT.

    Product # :

    PRO-2151

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    Description

    OPTC Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 336 amino acids (20-332 a.a) and having a molecular mass of 37.6kDa. OPTC is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    OPTC protein solution (0.5mg/ml) containing 20mM Tris-HCl (pH8.0) and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Opticin also known as OPTC is a member of the class III of the small leucine-rich repeat protein (SLRP) family. Members of this family are usually linked with the extracellular matrix. OPTC is attended in significant quantities in the vitreous of the eye and also localizes to the cornea, iris, ciliary body, optic nerve, choroid, retina, and fetal liver. OPTC might noncovalently bind collagen fibrils and regulate fibril morphology, spacing and organization. OPTC is mapped to a an area of chromosome 1 which is linked with the inherited eye diseases age-related macular degeneration (AMD) and posterior column ataxia with retinosa pigmentosa (AXPC1).

    • Synonyms

      Opticin, Oculoglycan, OPT.

    • 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 MGSASLPRKE RKRREEQMPR EGDSFEVLPL RNDVLNPDNY GEVIDLSNYE ELTDYGDQLP EVKVTSLAPA TSISPAKSTT APGTPSSNPT MTRPTTAGLL LSSQPNHGLP TCLVCVCLGS SVYCDDIDLE DIPPLPRRTA YLYARFNRIS RIRAEDFKGL TKLKRIDLSN NLISSIDNDA FRLLHALQDL ILPENQLEAL PVLPSGIEFL DVRLNRLQSS GIQPAAFRAM EKLQFLYLSD NLLDSIPGPL PLSLRSVHLQ NNLIETMQRD VFCDPEEHKH TRRQLEDIRL DGNPINLSLF PSAYFCLPRL PIGRFT.

    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.

    Optc Human
  • View Data Sheet

    Name :

    OTUB1 Human

    Description:

    Ubiquitin Aldehyde Binding 1 Human Recombinant

    Ubiquitin thioesterase OTUB1, Otubain-1, OTU domain-containing ubiquitin aldehyde-binding protein 1, Ubiquitin-specific-processing protease OTUB1, Deubiquitinating enzyme OTUB1, OTUB1, OTB1, OTU1, HSPC263, MGC4584, FLJ20113, FLJ40710, MGC111158.

    Product # :

    PRO-711

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    Description

    OTUB1 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 291 amino acids (1- 271 a.a.) and having a molecular mass of 33.4kDa.The OTUB1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The OTUB1 solution contains 20mM Tris buffer (pH 8.0) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Otubain 1 (OTUB1) belongs to the ovarian tumor (OUT) superfamily of predicted cysteine proteases and inhibits cytokine gene transcription in the immune system through its interaction with a ubiquitin protease and E3 ubiquitin ligase. OTUB1 is a highly specific ubiquitin iso-peptidase, it cleaves ubiquitin from branched poly-ubiquitin chains but not from ubiquitinated substrates. OTUB1 is believed to work in specific ubiquitin-dependent pathways, possibly by providing an editing function of polyubiquitin chain growth. OTUB1 is a hydrolase that removes conjugated ubiquitin from proteins in vitro and may therefore have a significant regulatory role in the level of protein turnover by preventing degradation. Additionally, OTUB1 is a regulator of T-cell anergy, a phenomenon that occurs when T-cells are rendered impassive to antigen re-challenge and no longer respond to their cognate antigen. OTUB1 acts via its interaction with RNF128/GRAIL, which is an essential inductor of CD4 T-cell anergy.

    • Synonyms

      Ubiquitin thioesterase OTUB1, Otubain-1, OTU domain-containing ubiquitin aldehyde-binding protein 1, Ubiquitin-specific-processing protease OTUB1, Deubiquitinating enzyme OTUB1, OTUB1, OTB1, OTU1, HSPC263, MGC4584, FLJ20113, FLJ40710, MGC111158.

    • 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 MAAEEPQQQK QEPLGSDSEG VNCLAYDEAI MAQQDRIQQE IAVQNPLVSE RLELSVLYKE YAEDDNIYQQ KIKDLHKKYS YIRKTRPDGN CFYRAFGFSH LEALLDDSKE LQRFKAVSAK SKEDLVSQGF TEFTIEDFHN TFMDLIEQVE KQTSVADLLA SFNDQSTSDY LVVYLRLLTS GYLQRESKFF EHFIEGGRTV KEFCQQEVEP MCKESDHIHI IALAQALSVS IQVEYMDRGE GGTTNPHIFP EGSEPKVYLL YRPGHYDILY K.

    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.

    Otub1 Human
  • View Data Sheet

    Name :

    ETHE1 Human

    Description:

    Ethylmalonic Encephalopathy 1 Human Recombinant

    Ethylmalonic encephalopathy protein 1, HSCO, Hepatoma subtracted clone one protein, YF13H12, protein ETHE1 mitochondrial, D83198, EC 3.1.2.6.

    Product # :

    PRO-1027

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    Description

    ETHE1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 267 amino acids (13-254) and having a molecular mass of 29.1kDa.ETHE1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The ETHE1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      ETHE1 is a mitochondrial sulfur dioxygenase involved in catabolism of sulfide that accumulates to toxic levels in ethylmalonic encephalopathy. Mutations of ETHE1 were detected in all the typical ethylmalonic encephalopathy patients analysed, but no ETHE1 mutations were identified in patients presenting with early onset progressive encephalopathy with ethylmalonic aciduria.

    • Synonyms

      Ethylmalonic encephalopathy protein 1, HSCO, Hepatoma subtracted clone one protein, YF13H12, protein ETHE1 mitochondrial, D83198, EC 3.1.2.6.

    • 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 MGSHMLSQRG GSGAPILLRQ MFEPVSCTFT YLLGDRESRE AVLIDPVLET APRDAQLIKE LGLRLLYAVN THCHADHITG SGLLRSLLPG CQSVISRLSG AQADLHIEDG DSIRFGRFAL ETRASPGHTP GCVTFVLNDH SMAFTGDALL IRGCGRTDFQ QGCAKTLYHS VHEKIFTLPG DCLIYPAHDY HGFTVSTVEE ERTLNPRLTL SCEEFVKIMG NLNLPKPQQI DFAVPANMRC GVQTPTA

    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.

    Ethe1 Human
  • View Data Sheet

    Name :

    TCEAL3 Human

    Description:

    Transcription Elongation Factor A (SII)-Like 3 Human Recombinant

    Transcription elongation factor A (SII)-like 3, TCEA-like protein 3, MGC15737.

    Product # :

    PRO-1128

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    Description

    TCEAL3 Human Recombinant produced in E. coli is a single polypeptide chain containing 224 amino acids (1-200) and having a molecular mass of 25.0 kDa.TCEAL3 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The TCEAL3 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      TCEAL3 belongs to the transcription elongation factor A (SII)-like (TCEAL) gene family. TCEAL family members hold TFA domains and operate as nuclear phosphoproteins which control transcription in a promoter context-dependent fashion. Various family members are situated in the X chromosome.

    • Synonyms

      Transcription elongation factor A (SII)-like 3, TCEA-like protein 3, MGC15737.

    • 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 MGSHMEKPYN KNEGNLENEG KPEDEVEPDD EGKSDEEEKP DVEGKTECEG KREDEGEPGD EGQLEDEGSQ EKQGRSEGEG KPQGEGKPAS QAKPESQPRA AEKRPAEDYV PRKAKRKTDR GTDDSPKDSQ EDLQERHLSS EEMMRECGDV SRAQEELRKK QKMGGFHWMQ RDVQDPFAPR GQRGVRGVRG GGRGQRGLHD IPYL

    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.

    Tceal3 Human
  • View Data Sheet

    Name :

    PINX1 Human

    Description:

    PIN2-Interacting Protein 1 Human Recombinant

    PINX1, LPTL, LPTS, MGC8850, FLJ20565, Pin2-interacting protein X1, TRF1-interacting protein 1, Liver-related putative tumor suppressor, Protein 67-11-3.

    Product # :

    PRO-693

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    Description

    Recombinant Human PINX1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 348 amino acids (1-328 a.a) and having a molecular mass of 39.1 kDa. PINX1 is fused to 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PINX1 protein contains 20mM Tris-HCl buffer pH-8, 1mM DTT and 10% glycerol.

    Purity

    Greater than 95.0% as determined by analysis by SDS-PAGE.

    More Info

    • Introduction

      PINX1 is a common expressed protein that localizes to nucleoli and telomere speckles. PINX1 contains a Telomerase Inhibiting Domain that is caable of binding MCRS1, TERT and TERF1. PINX1 has been shown to be a potent telomerase inhibitor and putative tumor suppressor. PINX1 is recruited to chromosome periphery by Nucleolin, their complex is necessary for faithful chromosome congression. PINX1 regulates the nucleolar accumulation and telomeric association of TRF1. PINX1 is involved in gastric cancer development. PINX1 expression is a sign of gastric cancer development. Constitutive expression of PINX1 attributes to telomere maintenance by telomerase and tumorigenicity in cancer cells.

    • Synonyms

      PINX1, LPTL, LPTS, MGC8850, FLJ20565, Pin2-interacting protein X1, TRF1-interacting protein 1, Liver-related putative tumor suppressor, Protein 67-11-3.

    • 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 MSMLAERRRK QKWAVDPQNT AWSNDDSKFG QRMLEKMGWS KGKGLGAQEH GATDHIKVQV KNNHLGLGAT INNEDNWIAH QDDFNQLLAE LNTCHGQETT DSSDKKEKKS FSLEEKSKIS KNRVHYMKFT KGKDLSSRSK TDLDCIFGKR QSKKTPEGDA SPSTPEENET TTTSAFTIQE YFAKRMAALK NKPQVPVPGS DISETQVERK RGKKINKEAT GKDVESYLQP KAKRHTEGKP ERAEAQERVA KKKSAPAEEQ LRGPCWDQSS KASAQDAGDH VQPPEGRDFT LKPKKRRGKK KLQKPVEIAE DATLEETLVK KKKKKDSK.

    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.

    Pinx1 Human
  • View Data Sheet

    Name :

    Activin B Human

    Description:

    Activin-B Human Recombinant

    Inhibin beta B (activin AB beta polypeptide), Inhibin, beta-2, Activin beta-B chain, MGC157939.

    Product # :

    CYT-058

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    Description

    Activin B human Recombinant produced in Nicotiana benthamiana plant is a beta-B single chain (aa 293-406) containing 123 amino acids (molecular formula C615H910N178O177S12). Activin B is fused to a 10-His-tag at the N-terminal having the total molecular mass of 14kDa and purified by standard chromatographic techniques.

    Source

    Nicotiana benthamiana plant

    Formulation

    Lyophilized from 1mg/ml solution in 0.05M Tris-HCl buffer pH 7.4.

    Purity

    Greater than 97.0% as determined by Analysis by SDS-PAGE.

    More Info

    • Introduction

      Inhibins are dimeric peptide hormones produced by female ovarian granulose cells and male Sertoli cells as well as a variety of other tissues. Inhibins have two isoforms, A and B, with the same alpha subunit but different beta subunits. Inhibin A is a dimer of alpha and beta A subunits, inhibin B is a dimer of alpha and beta B subunits.
      Inhibins are thought to inhibit the production of follicle-stimulating hormone (FSH) by the pituitary gland. In addition, Inhibins are also thought to play a role in the control of gametogenesis, and embryonic and fetal development.

    • Synonyms

      Inhibin beta B (activin AB beta polypeptide), Inhibin, beta-2, Activin beta-B chain, MGC157939.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Activin B although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Activin B 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 Activin B in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      HHHHHHHHHH GLECDGRTNL CCRQQFFIDF RLIGWNDWII APTGYYGNYC EGSCPAYLAG VPGSASSFHT AVVNQYRMRG LNPGTVNSCC IPTKLSTMSM LYFDDEYNIV KRDVPNMIVE ECG

    • Background

      What is the molecular weight / Mw of Activin B Protein?
      Activin A Protein has a total Mw of 14 kDa.

      What is the source or expression system of Activin B Protein?
      Nicotinia

      What is the Purity of Activin B Protein?
      Activin B Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of Activin B Protein?
      The biological functionality of Activin-B Protein will be determined in the future.

      What is the endotoxin level for Activin B Protein?
      The endotoxin level is minimal, ACTIVIN B Protein was purified using conventional chromatography techniques.

      What is the amino acid sequence of ACTIVIN B Protein?
      HHHHHHHHHH GLECDGRTNL CCRQQFFIDF RLIGWNDWII APTGYYGNYC EGSCPAYLAG VPGSASSFHT AVVNQYRMRG LNPGTVNSCC IPTKLSTMSM LYFDDEYNIV KRDVPNMIVE ECG

      What applications can ACTIVIN B Protein be used in?

      ACTIVIN A Protein can probably be used in western blot, ELISA and Lateral Flow.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Activin B Human Plant
  • View Data Sheet

    Name :

    Betacellulin His Human

    Description:

    Betacellulin Human Recombinant, His Tag

    Betacellulin, Probetacellulin. 

    Product # :

    CYT-077

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    • sds-page

    Description

    BTC Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 101 amino acids (32-111) and having a molecular mass of 11.3 kDa.BTC is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The BTC solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 5mM DTT, 0.2M NaCl and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    sds-page

    Betacellulin-sds-page - Product image 1

    More Info

    • Introduction

      Btc is a potent mitogen for retinal pigment epithelial cells and vascular smooth muscle cells. The effects of betacellulin are probably mediated by the egf receptor and other related receptors.

    • Synonyms

      Betacellulin, Probetacellulin.

    • 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 MDGNSTRSPE TNGLLCGDPE ENCAATTTQS KRKGHFSRCP KQYKHYCIKG RCRFVVAEQT PSCVCDEGYI GARCERVDLF Y

    • Background

      What is the molecular weight/Mw of BETACELLULIN Protein?
      BETACELLULIN Protein has a total Mw of 11.3kDa.

      What is the source or expression system of BETACELLULIN Protein?
      Escherichia Coli.

      What is the Purity of BETACELLULIN Protein?
      BETACELLULIN Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of BETACELLULIN Protein?
      The biological functionality of BETACELLULIN Protein will be determined in the future.

      What is the amino acid sequence of BETACELLULIN Protein?
      MGSSHHHHHH SSGLVPRGSH MDGNSTRSPE TNGLLCGDPE ENCAATTTQS KRKGHFSRCP KQYKHYCIKG RCRFVVAEQT PSCVCDEGYI GARCERVDLF Y

      What applications can BETACELLULIN Protein be used in?
      BETACELLULIN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for BETACELLULIN Protein?
      The endotoxin level is minimal, BETACELLULIN 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.

    Btc His Human
  • View Data Sheet

    Name :

    Hemopexin Human, Sf9

    Description:

    Hemopexin Human Recombinant, Sf9

    Hemopexin, Beta-1B-Glycoprotein, HX, Beta-1B-glycoprotein.

    Product # :

    PRO-2544

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    Description

    Hemopexin produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 448 amino acids (24-462a.a.) and having a molecular mass of 50.4kDa. (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).Hemopexin is expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    Hemopexin protein solution (0.5mg/ml) contains 10% glycerol & Phosphate Buffered Saline (pH 7.4).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Hemopexin (or haemopexin) is a plasma protein that binds heme with the highest affinity of any known protein. Hemopexin is generally expressed in liver, and belongs to acute phase reactants, the synthesis of which is induced after inflammation. Heme is potentially very toxic because of its ability to intercalate into lipid membrane and to generate hydroxyl radicals. Hemopexin’s function of scavenging the heme released or lost by the turnover of heme proteins such as hemoglobin defends the body from the oxidative damage that free heme can cause. Additionally, hemopexin discharges its bound ligand for internalisation upon interacting with a specific receptor located on the surface of liver cells. This hemopexin function is in order to preserve the body's iron. Hemopexin’s levels in the serum are an indication of how much heme is present in the blood. Low Hemopexin levels show that there is a lot of it in the serum. For that reason, low hemopexin levels indicate that there has been consid

    • Synonyms

      Hemopexin, Beta-1B-Glycoprotein, HX, Beta-1B-glycoprotein.

    • 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

      ADPTPLPPTS AHGNVAEGET KPDPDVTERC SDGWSFDATT LDDNGTMLFF KGEFVWKSHK WDRELISERW KNFPSPVDAA FRQGHNSVFL IKGDKVWVYP PEKKEKGYPK LLQDEFPGIP SPLDAAVECH RGECQAEGVL FFQGDREWFW DLATGTMKER SWPAVGNCSS ALRWLGRYYC FQGNQFLRFD PVRGEVPPRY PRDVRDYFMP CPGRGHGHRN GTGHGNSTHH GPEYMRCSPH LVLSALTSDN HGATYAFSGT HYWRLDTSRD GWHSWPIAHQ WPQGPSAVDA AFSWEEKLYL VQGTQVYVFL TKGGYTLVSG YPKRLEKEVG TPHGIILDSV DAAFICPGSS RLHIMAGRRL WWLDLKSGAQ ATWTELPWPH EKVDGALCME KSLGPNSCSA NGPGLYLIHG PNLYCYSDVE KLNAAKALPQ PQNVTSLLGC THHHHHHH.

    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.

    Hemopexin Protein
  • View Data Sheet

    Name :

    IL 11 Human

    Description:

    Interleukin-11 Human Recombinant

    AGIF, Adipogenesis inhibitory factor, IL-11.

    Product # :

    CYT-214

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

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    More Info

    • description
    • source
    • formulation
    • purity
    • biological activity
    • More Info

    Description

    Interleukin-11 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 179 amino acids and having a molecular mass of 19256.29 Dalton. The IL-11 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution with no additives.

    Purity

    Greater than 98.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The ED50 as determined by the dose-dependant stimulation of the proliferation of murine 7TD1 was found to be < 10ng/ml, corresponding to a Specific Activity of 100,000 IU/mg.

    More Info

    • Introduction

      IL11 is a member of the gp130 family of cytokines. These cytokines drive the assembly of multisubunit receptor complexes, all of which contain at least one molecule of the transmembrane signaling receptor IL6ST (gp130). IL-11 is shown to stimulate the T-cell-dependent development of immunoglobulin-producing B cells. It is also found to support the proliferation of hematopoietic stem cells and megakaryocyte progenitor cells.

    • Synonyms

      AGIF, Adipogenesis inhibitory factor, IL-11.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Interleukin-11 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL11 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 Interleukin 11 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      The sequence of the first five N-terminal amino acids was determined and was found to be Gly-Pro-Pro-Pro-Gly. N-terminal methionine has been completely removed enzymatically.

    • Protein content

      Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.95 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a calibrated solution of IL-11 as a Reference Standard.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Il 11 Human
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