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Search results

1000 results found for “Hemoglobin”

Name

Description

Product #

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  • View Data Sheet

    Name :

    GALM Human

    Description:

    Galactose Mutarotase Human Recombinant

    Aldose 1-epimerase, BLOCK25, IBD1, EC=5.1.3.3, GALM, galactose mutarotase.

    Product # :

    ENZ-541

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    Description

    GALM Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 362 amino acids (1-342 a.a.) and having a molecular mass of 39.9 kDa. The GALM is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GALM solution (1mg/ml) contains 20mM Tris-HCl (pH 8.0) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      GALM is a main enzyme of carbohydrate metabolism catalysing the translation of beta-D-galactose to alpha-D-galactose. GALM is needed for normal galactose metabolism by preserveing the equilibrium of alpha and beta anomers of galactose. GALM is required for the production of complex oligosaccharides.

    • Synonyms

      Aldose 1-epimerase, BLOCK25, IBD1, EC=5.1.3.3, GALM, galactose mutarotase.

    • 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 MASVTRAVFG ELPSGGGTVE KFQLQSDLLR VDIISWGCTI TALEVKDRQG RASDVVLGFA ELEGYLQKQP YFGAVIGRVA NRIAKGTFKV DGKEYHLAIN KEPNSLHGGV RGFDKVLWTP RVLSNGVQFS RISPDGEEGY PGELKVWVTY TLDGGELIVN YRAQASQATP VNLTNHSYFN LAGQASPNIN DHEVTIEADT YLPVDETLIP TGEVAPVQGT AFDLRKPVEL GKHLQDFHLN GFDHNFCLKG SKEKHFCARV HHAASGRVLE VYTTQPGVQF YTGNFLDGTL KGKNGAVYPK HSGFCLETQN WPDAVNQPRF PPVLLRPGEE YDHTTWFKFS VA.

    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.

    Galm Human
  • View Data Sheet

    Name :

    CDC123 Human

    Description:

    Cell Division Cycle 123 Human Recombinant

    C10orf7, D123, Cell division cycle protein 123 homolog, Protein D123, HT-1080, PZ32, Chromosome 10 Open Reading Frame 7.

    Product # :

    PRO-1463

    Price :

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    Description

    CDC123 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 359 amino acids (1-336 a.a) and having a molecular mass of 41.5kDa.CDC123 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CDC123 protein solution (0. 5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 2mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CDC123 is a member of the CDC123 family. CDC123is required for S phase entry of the cell cycle. It is also broadly expressed in spleen,thymus, prostate, testis, ovary, small intestine, colon and leukocytes with the uppermost expression in testis.

    • Synonyms

      C10orf7, D123, Cell division cycle protein 123 homolog, Protein D123, HT-1080, PZ32, Chromosome 10 Open Reading Frame 7.

    • 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 MGSMKKEHVL HCQFSAWYPF FRGVTIKSVI LPLPQNVKDY LLDDGTLVVS GRDDPPTHSQ PDSDDEAEEI QWSDDENTAT LTAPEFPEFA TKVQEAINSL GGSVFPKLNW SAPRDAYWIA MNSSLKCKTL SDIFLLFKSS DFITRDFTQP FIHCTDDSPD PCIEYELVLR KWCELIPGAE FRCFVKENKL IGISQRDYTQ YYDHISKQKE EIRRCIQDFF KKHIQYKFLD EDFVFDIYRD SRGKVWLIDF NPFGEVTDSL LFTWEELISE NNLNGDFSEV DAQEQDSPAF RCTNSEVTVQ PSPYLSYRLP KDFVDLSTGE DAHKLIDFLK LKRNQQEDD

    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.

    Cdc123 Human
  • View Data Sheet

    Name :

    TTC1 Human

    Description:

    Tetratricopeptide Repeat Domain 1 Human Recombinant

    Tetratricopeptide repeat protein 1, TPR repeat protein 1, TTC1, TPR1.

    Product # :

    PRO-1160

    Price :

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    Description

    TTC1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 316 amino acids (1-292 a.a) and having a molecular mass of 36.1kDa (Molecular weight on SDS-PAGE will appear higher).TTC1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TTC1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Tetratricopeptide repeat protein 1 (TTC1) is comprised of 292 amino acids with 3 TPR motifs, such as a Galpha16-binding protein. This interaction is confirmed both in vitro and in transfected mammalian cells, where TTC1 also binds to a number of other Galpha proteins. TTC1 interacts with Ha-Ras especially in its active form. TTC1 also interacts with the GAP domain of NF1.

    • Synonyms

      Tetratricopeptide repeat protein 1, TPR repeat protein 1, TTC1, TPR1.

    • 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 MGSHMGEKSE NCGVPEDLLN GLKVTDTQEA ECAGPPVPDP KNQHSQSKLL RDDEAHLQED QGEEECFHDC SASFEEEPGA DKVENKSNED VNSSELDEEY LIELEKNMSD EEKQKRREES TRLKEEGNEQ FKKGDYIEAE SSYSRALEMC PSCFQKERSI LFSNRAAARM KQDKKEMAIN DCSKAIQLNP SYIRAILRRA ELYEKTDKLD EALEDYKSIL EKDPSIHQAR EACMRLPKQI EERNERLKEE MLGKLKDLGN LVLRPFGLST ENFQIKQDSS TGSYSINFVQ NPNNNR.

    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.

    Ttc1 Human
  • View Data Sheet

    Name :

    UBL3 Human

    Description:

    Ubiquitin-Like 3 Human Recombinant

    Ubiquitin-like 3, FLJ32018, HCG-1, Membrane-anchored ubiquitin-fold protein, MUB, PNSC1, HsMUB, DKFZP434K151.

    Product # :

    PRO-230

    Price :

    Quantity :

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    Description

    UBL3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 134 amino acids (1-114a.a) and having a molecular mass of 15.0kDa.UBL3 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    UBL3 protein solution (1mg/1ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 2mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      UBL3 - a member of the ubiquitin-like family is found in the membrane. UBL3 holds two N-glycosylation sites, a C-terminal prenylation site and a protein kinase C phosphorylation site. Even though Ubiquitin-like proteins are not directly involved in protein degradation, it seems they have several mechanistic similarities to the ubiquitin pathway.

    • Synonyms

      Ubiquitin-like 3, FLJ32018, HCG-1, Membrane-anchored ubiquitin-fold protein, MUB, PNSC1, HsMUB, DKFZP434K151.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      UBL3 although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MSSNVPADMI NLRLILVSGK TKEFLFSPND SASDIAKHVY DNWPMDWEEE QVSSPNILRL IYQGRFLHGN VTLGALKLPF GKTTVMHLVA RETLPEPNSQ GQRNREKTGE SNCC

    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.

    Ubl3 Human
  • View Data Sheet

    Name :

    UBL5 Human

    Description:

    Ubiquitin-Like 5 Human Recombinant

    Ubiquitin-like protein 5, HUB1, FLJ46917, MGC131795.

    Product # :

    PRO-231

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    Description

    UBL5 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 93 amino acids (1-73a.a) and having a molecular mass of 10.7kDa.UBL3 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    UBL5 protein solution (1mg/1ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 2mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      UBL5 is believed to be a reversible modulator of protein function unlike ubiquitin which is a protein degrader. UBL5 influences a nuclear phase obligatory for increasing a reaction against the risk of mitochondrial protein misfolding.

    • Synonyms

      Ubiquitin-like protein 5, HUB1, FLJ46917, MGC131795.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      UBL5 although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MIEVVCNDRL GKKVRVKCNT DDTIGDLKKL IAAQTGTRWN KIVLKKWYTI FKDHVSLGDY EIHDGMNLEL YYQ

    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.

    Ubl5 Human
  • View Data Sheet

    Name :

    CCL22 Human

    Description:

    Macrophage-Derived Chemokine Human Recombinant (CCL22)

    C-C motif chemokine 22, Small-inducible cytokine A22, Macrophage-derived chemokine, MDC(1-69), Stimulated T-cell chemotactic protein 1, CC chemokine STCP-1, CCL22, MDC, SCYA22, ABCD-1, DC/B-CK, MGC34554, A-152E5.1.

    Product # :

    CHM-250

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    Description

    MDC Human Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 69 amino acids and having a molecular mass of 8.1 kDa. The MDC is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CCL22 filtered (0.4µm) and lyophilized from a concentrated solution containing 20mM phosphate buffer & 500mM NaCl pH-7.4.

    Purity

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

    Biological Activity

    Determined by its ability to chemoattract human T cells using a concentration range of 10ng-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.

    More Info

    • Introduction

      MDC (CCL22) is a small cytokine that belongs to the CC chemokine family. CCL22 is one of several Cys-Cys (CC) cytokine genes clustered on the q arm of chromosome 16.
      MDC shows chemotactic activity for natural killer cells, chronically activated T lymphocytes, monocytes and dendritic cells. On the other hand, MDC shows a mild activity for primary activated T lymphocytes and has no chemoattractant activity for neutrophils, eosinophils and resting T lymphocytes. MDC may also have a role in the trafficking of activated T lymphocytes to inflammatory sites and other aspects of activated T lymphocyte physiology. MDC interacts with cell surface chemokine receptors CCR4.
      CCL22 is vastly expressed in macrophage and in monocyte-derived dendritic cells, and thymus. CCL22 is also found in the lymph node, appendix, activated monocytes, resting and activated macrophages. Lower expression of CCL22 can be seen in the lung and the spleen and very weak expression in the small intestine. In the lymph node CCL22 is expressed in a mature subset of Langerhans' cells (CD1a+ and CD83+).
      Furthermore, CCL22 is expressed in atopic dermatitis, allergic contact dermatitis skin, and psoriasis, in both the epidermis and dermis. In addition, MDC has a role in hindering progression of lung cancer. Moreover, significantly higher CCL22 expression is linked to gastric cancer.

    • Synonyms

      C-C motif chemokine 22, Small-inducible cytokine A22, Macrophage-derived chemokine, MDC(1-69), Stimulated T-cell chemotactic protein 1, CC chemokine STCP-1, CCL22, MDC, SCYA22, ABCD-1, DC/B-CK, MGC34554, A-152E5.1.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized CCL22 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL22 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 CCL22 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      GPYGANMEDS VCCRDYVRYR LPLRVVKHFY WTSDSCPRPG VVLLTFRDKE ICADPRVPWV KMILNKLSQ.

    • Background

      What is the molecular weight/Mw of CCL22 HUMAN Protein?
      CCL22 HUMAN Protein has a total Mw of 8.1kDa.

      What is the source or expression system of CCL22 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of CCL22 HUMAN Protein?
      CCL22 HUMAN Protein is > 97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCL22 HUMAN Protein?
      Determined by its ability to chemoattract human T cells using a concentration range of 10ng-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.

      What is the amino acid sequence of CCL22 HUMAN Protein?
      GPYGANMEDS VCCRDYVRYR LPLRVVKHFY WTSDSCPRPG VVLLTFRDKE ICADPRVPWV KMILNKLSQ.

      What applications can CCL22 HUMAN Protein be used in?
      CCL22 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CCL22 HUMAN Protein?
      The endotoxin level is minimal, CCL22 HUMAN Protein was purified using conventional chromatography techniques.

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    Mdc Human
  • View Data Sheet

    Name :

    4 1BBL Human, His

    Description:

    4-1BB Ligand Human Recombinant, His Tag

    CD137L, CD137-L, 4-1BBL, 4-1BB Ligand, TNFSF9, Tumor Necrosis Factor (ligand) Superfamily Member 9.

    Product # :

    CYT-649

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    • sds-page

    Description

    TNFSF9 Human Recombinant fused to 37 amino acids His tag at N-terminus produced in E.Coli is a single, non-glycosylated polypeptide chain containing 222 amino acids (71-254 a.a.) and having a molecular mass of 23.8 kDa. The TNFSF9 37 aa His tag fusion protein is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Recombinant 4-1BBL solution (1mg/ml) contains 20mM Tris-HCl buffer pH-8, 100mM NaCl and 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE

    sds-page

    4-1BBL-His-sds-page - Product image 1

    More Info

    • Introduction

      4-1BBL is a transmembrane cytokine that is part of the tumor necrosis factor (TNF) ligand family. 4-1BBL is a bidirectional signal transducer that performs as a ligand for TNFRSF9, which is a costimulatory receptor molecule in T lymphocytes. TNFSF9 and its TNFRSF9 take part in the antigen presentation development and in the generation of cytotoxic T cells. 4-1BBR is absent from resting T lymphocytes but rapidly expressed upon antigenic stimulation. TNFSF9 reactivates anergic T lymphocytes as well as promoting T lymphocyte proliferation. 4-1BB Ligand is needed for the optimal CD8 responses in CD8 T cells. 4-1BBL is expressed in carcinoma cell lines, and is thought to be involved in T cell-tumor cell interaction. 4-1BBL is expressed by activated B cells, macrophages, dendritic cells, activated T cells, neurons and astrocytes. The interaction of 4-1BB with TNFRSF9 strongly regulates immunity and has been proposed to preferentially control T cell responses based on studies in various murin

    • Synonyms

      CD137L, CD137-L, 4-1BBL, 4-1BB Ligand, TNFSF9, Tumor Necrosis Factor (ligand) Superfamily Member 9.

    • 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

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMRE GPELSPDDPA GLLDLRQGMF AQLVAQNVLL IDGPLSWYSD PGLAGVSLTGGLSYKEDTKE LVVAKAGVYY VFFQLELRRV VAGEGSGSVS LALHLQPLRS AAGAAALALT VDLPPASSEA RNSAFGFQGR LLHLSAGQRL GVHLHTEARA RHAWQLTQGA TVLGLFRVTP EIPAGLPSPR SE.

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    4-1Bbl Protein
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    Name :

    RHEB Human

    Description:

    Ras Homolog Enriched in Brain Human Recombinant

    Ras homolog enriched in brain, RHEB2, Ras homolog enriched in brain, GTP-binding protein Rheb, RheB, Ras homolog enriched in brain GTP binding protein Rheb, Ras homolog enriched in brain 2, RHEB 2.

    Product # :

    PRO-308

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    Description

    RHEB Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 197 amino acids (1-181 amino acids) and having a molecular mass of 21.7 kDa.The RHEB is fused to T7-tag at N-terminus (16 a.a.) and is purified by standard chromatography techniques.

    Source

    Escherichia Coli.

    Formulation

    The RHEB protein solution (1mg/ml) contains 20mM Tris-HCl pH-8, 1mM DTT and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      RHEB is part of the Ras & GTPase superfamily that was originally identified as an immediate-early gene in brain but is also widely expressed in other tissues. RHEB encodes a lipid-anchored, cell membrane protein with five repeats of the RAS-related GTP-binding region. RHEB is necessary in regulation of growth and cell cycle progression due to its role in the TOR/S6K signaling pathway. RHEB has GTPase activity and shuttles between a GDP-bound form and a GTP-bound form, and farnesylation of the protein is required for this activity. RHEB induces oncogenic transformation. RHEB overexpression accelerates lymphomagenesis and is associated with prostate cancer. RHEB can cytopathologically distinguish between fibroadenoma from malignant breast carcinomas which is considered as a secondary diagnostic tool. RHEB has a central role in the regulation of the Ras/B-Raf/C-Raf/MEK signaling network.

    • Synonyms

      Ras homolog enriched in brain, RHEB2, Ras homolog enriched in brain, GTP-binding protein Rheb, RheB, Ras homolog enriched in brain GTP binding protein Rheb, Ras homolog enriched in brain 2, RHEB 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

      MASMTGGQQM GRGSASMPQS KSRKIAILGY RSVGKSSLTI QFVEGQFVDS YDPTIENTFT KLITVNGQEY HLQLVDTAGQ DEYSIFPQTY SIDINGYILV YSVTSIKSFE VIKVIHGKLL DMVGKVQIPI MLVGNKKDLH MERVISYEEG KALAESWNAA FLESSAKENQ TAVDVFRRII LEAEKMDGAA SQGKSSC.

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    Rheb Human
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    Name :

    SNRPC Human

    Description:

    Small Nuclear Ribonucleoprotein Polypeptide C Human Recombinant

    U1 small nuclear ribonucleoprotein C, U1 snRNP C, U1-C, U1C, SNRPC, Yhc1.

    Product # :

    PRO-1004

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    Description

    SNRPC Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 182 amino acids (1-159 a.a.) and having a molecular mass of 19.8kDa (Molecular weight on SDS-PAGE will appear higher).SNRPC is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SNRPC protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 50% glycerol, 0.3M NaCl, 5mM DTT and 2mM EDTA.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      SNRPC is a member of the U1 small nuclear ribonucleoprotein C family. The SNRPC protein component of the U1 small nuclear ribonucleoprotein (snRNP) particle required for the formation of the spliceosome. SNRPC participates in the processing of nuclear precursor messenger RNA splicing. snRNP particles are tackled by autoantibodies frequently produced by patients with connective tissue diseases.

    • Synonyms

      U1 small nuclear ribonucleoprotein C, U1 snRNP C, U1-C, U1C, SNRPC, Yhc1.

    • 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 MGSMPKFYCD YCDTYLTHDS PSVRKTHCSG RKHKENVKDY YQKWMEEQAQ SLIDKTTAAF QQGKIPPTPF SAPPPAGAMI PPPPSLPGPP RPGMMPAPHM GGPPMMPMMG PPPPGMMPVG PAPGMRPPMG GHMPMMPGPP MMRPPARPMM VPTRPGMTRP DR.

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    Snrpc Human
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    Name :

    ProInsulin Human

    Description:

    ProInsulin C-Peptide Analogue Human Recombinant

    Insulin, Insulin-Dependent Diabetes Mellitus 2, Preproinsulin, Proinsulin, MODY10, IDDM1, IDDM2, IDDM, ILPR, IRDN. 

    Product # :

    CYT-1120

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    Description

    ProInsulin C-Peptide Analogue Human Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 35 amino acid and having a molecular mass of approximately 3.6kDa.ProInsulin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2μm filtered concentrated solution in PBS, pH 7.4.

    Purity

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

    More Info

    • Introduction

      Insulin decreases blood glucose concentration. Insulin increases cell permeability to monosaccharides, amino acids and fatty acids. Insulin accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver.

    • Synonyms

      Insulin, Insulin-Dependent Diabetes Mellitus 2, Preproinsulin, Proinsulin, MODY10, IDDM1, IDDM2, IDDM, ILPR, IRDN.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      RREAEDLQVG QVELGGGPGA GSLQPLALEG SLQKR.

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    Proinsulin C Peptide
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    Name :

    UBD Human

    Description:

    Ubiquitin-D Human Recombinant

    Ubiquitin D, Diubiquitin, Ubiquitin-like protein FAT10, UBD, FAT10, UBD-3, GABBR1.

    Product # :

    PRO-927

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    Description

    UBD Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 188 amino acids (1-165 a.a.) and having a molecular mass of 20.9kDa.UBD is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    UBD protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 40% glycerol, 0.15M NaCl and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Ubiquitin D (UBD) is an ubiquitin-like modifier (UBL) of the ubiquitin protein family. UBD is an ubiquitin-like protein which can form covalent conjugates, thus targeting proteins for degradation by the 26S proteasome. It is assumed that, UBD has roles in regulation of cell cycle, innate immunity, and apoptosis. UBD is a TNF-a inducible ubiquitin-like protein with a presumed role in the immune response.

    • Synonyms

      Ubiquitin D, Diubiquitin, Ubiquitin-like protein FAT10, UBD, FAT10, UBD-3, GABBR1.

    • 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 MGSMAPNASC LCVHVRSEEW DLMTFDANPY DSVKKIKEHV RSKTKVPVQD QVLLLGSKIL KPRRSLSSYG IDKEKTIHLT LKVVKPSDEE LPLFLVESGD EAKRHLLQVR RSSSVAQVKA MIETKTGIIP ETQIVTCNGK RLEDGKMMAD YGIRKGNLLF LACYCIGG.

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    Ubd Human
  • View Data Sheet

    Name :

    VAMP2 Human, (1-94)

    Description:

    Synaptobrevin-2 Human Recombinant, (1-94)

    Vesicle Associated Membrane Protein 2, Vesicle-Associated Membrane Protein 2, Synaptobrevin 2, VAMP-2, SYB2, Synaptobrevin-2.

    Product # :

    PRO-2644

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    Description

    VAMP2 Human Recombinant produced in e.coli is a single, non-glycosylated polypeptide chain containing 118 amino acids (1-94 a.a) and having a molecular mass of 12.8kDa. VAMP2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.Coli

    Formulation

    The VAMP2 solution (0.5mg/1ml) contains 0.1mM PMSF, 10% glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Synaptobrevin-2 or VAMP2 is a protein that has a proline-rich N-terminal part, highly conserved hydrophilic domain, a transmembrane anchor and a C-terminal.VAMP2 found in the transmembrane region of the cell, in the cytoplasmic surface of the synaptic vesicle. The protein is mainly found in the Langerhans islets in the pancreas and glomerular cells in the kidney. A SNARE complex is created within the protein’s N-terminal domain and the target membrane-associated T.

    • Synonyms

      Vesicle Associated Membrane Protein 2, Vesicle-Associated Membrane Protein 2, Synaptobrevin 2, VAMP-2, SYB2, Synaptobrevin-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 MGSHMSATAA TAPPAAPAGE GGPPAPPPNL TSNRRLQQTQ AQVDEVVDIM RVNVDKVLER DQKLSELDDR ADALQAGASQ FETSAAKLKR KYWWKNLK.

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    Synaptobrevin 2 Human
  • View Data Sheet

    Name :

    YWHAE Human, His

    Description:

    Tyr-3/Trp-5 Monooxygenase Activation Protein, Epsilon Human Recombinant, His Tag

    YWHAE, MDS, MDCR, KCIP-1, 14-3-3E, 14-3-3 Epsilon, FLJ45465, Tyr-3/Trp- 5 Monooxygenase Activation Protein Epsilon, HEL2, KCIP-1, MDCR, MDS.

    Product # :

    PKA-095

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    Description

    YWHAE Human Recombinant produced in E. coli is a single polypeptide chain containing 275 amino acids (1-255) and having a molecular mass of 31.3kDa. YWHAE is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The YWHAE solution (1mg/1ml) contains phosphate buffered Saline (pH7.4), 1mM DTT and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      The 14-3-3 family of proteins plays a key regulatory role in signal transduction, checkpoint control, apoptotic and nutrient-sensing pathways. 14-3-3 proteins are highly conserved and ubiquitously expressed. There are at least seven isoforms, β, γ, ε, σ, ζ, τ and η that have been identified in mammals. The 14-3-3 epsilon, a subtype of the 14-3-3 family of proteins, was thought to be brain and neuron-specific. It has been shown to interact with CDC25 phosphatases, RAF1 and IRS1 proteins, suggesting its role in diverse biochemical activities related to signal transduction, such as cell division and regulation of insulin sensitivity. It has also been implicated in the pathogenesis of small cell lung cancer.

    • Synonyms

      YWHAE, MDS, MDCR, KCIP-1, 14-3-3E, 14-3-3 Epsilon, FLJ45465, Tyr-3/Trp- 5 Monooxygenase Activation Protein Epsilon, HEL2, KCIP-1, MDCR, MDS.

    • 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 MDDREDLVYQ AKLAEQAERY DEMVESMKKV AGMDVELTVE ERNLLSVAYK NVIGARRASW RIISSIEQKE ENKGGEDKLK MIREYRQMVE TELKLICCDI LDVLDKHLIP AANTGESKVF YYKMKGDYHR YLAEFATGND RKEAAENSLV AYKAASDIAM TELPPTHPIR LGLALNFSVF YYEILNSPDR ACRLAKAAFD DAIAELDTLS EESYKDSTLI MQLLRDNLTL WTSDMQGDGE EQNKEALQDV EDENQ.

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    Ywhae Human His
  • View Data Sheet

    Name :

    PHF13 Human

    Description:

    PHD Finger Protein 13 Human Recombinant

    PHF5, SPOC1, PHD finger protein 13, Survival time-associated PHD finger protein in ovarian cancer 1, PHF13.

    Product # :

    PRO-1532

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    Description

    PHF13 Human Recombinant produced in E. coli is a single polypeptide chain containing 323 amino acids (1-300) and having a molecular mass of 36kDa. PHF13 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PHF13 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol, 2mM DTT, 1mM EDTA and 250mM Imidazole.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      PHD finger protein 13 (PHF13) is necessary for normal chromosome separation during mitosis and also for normal chromosome condensation during the early stages of mitosis. PHF13 modulates chromatin structure.

    • Synonyms

      PHF5, SPOC1, PHD finger protein 13, Survival time-associated PHD finger protein in ovarian cancer 1, PHF13.

    • 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 MGSMDSDSCA AAFHPEEYSP SCKRRRTVED FNKFCTFVLA YAGYIPYPKE ELPLRSSPSP ANSTAGTIDS DGWDAGFSDI ASSVPLPVSD RCFSHLQPTL LQRAKPSNFL LDRKKTDKLK KKKKRKRRDS DAPGKEGYRG GLLKLEAADP YVETPTSPTL QDIPQAPSDP CSGWDSDTPS SGSCATVSPD QVKEIKTEGK RTIVRQGKQV VFRDEDSTGN DEDIMVDSDD DSWDLVTCFC MKPFAGRPMI ECNECHTWIH LSCAKIRKSN VPEVFVCQKC RDSKFDIRRS NRSRTGSRKL FLD.

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    Phf13 Human
  • View Data Sheet

    Name :

    ESR2 Human

    Description:

    Estrogen Receptor 2 Human Recombinant

    Estrogen Receptor Beta.

    Product # :

    PRO-2838

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    Description

    The ESR2 Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The ESR2 His-Tagged Fusion Protein, produced in E. coli, is a 10kDa protein containing 101 amino acid residues of the ESR2 Human, 216-316 amino acids.

    Source

    Escherichia Coli.

    Formulation

    Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Synonyms

      Estrogen Receptor Beta.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized ESR2 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 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.

    • Amino Acid Sequence

      CGSR RERCGYRLVR RQRSADEQLH CAGKAKRSGGHAPRVRELLL DALSPEQLVL TLLEAEPPHV LISRPSAPFTEASMMMSLTKLADKELVHMI SWAKKI.

    • Background

      Estrogen Receptor 2 also known as ESR2 takes part in mediating the biological effects of estrogen, influencing various physiological and pathological processes. ESR2 is found in different tissues including the brain, reproductive organs, bones, cardiovascular system, and immune cells and has distinct functions. ESR2 is involved in various biological processes by responding to estrogen which is an important hormone in regulating reproductive and metabolic functions.

    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.

    Esr2 Protein
  • View Data Sheet

    Name :

    MET Human

    Description:

    Met Proto-Oncogene Human Recombinant

    Hepatocyte growth factor receptor, HGF receptor, HGF/SF receptor, Proto-oncogene c-Met, Scatter factor receptor, SF receptor, Tyrosine-protein kinase Met, MET,HGFR, AUTS9, RCCP2.

    Product # :

    PRO-207

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    Description

    Met Proto-Oncogene Human Recombinant produced in Insect cells amino acids 1039-1345, having a molecular weight of 34.6kDa.MET is purified by proprietary chromatographic techniques.

    Source

    Insect cells.

    Formulation

    MET protein (1mg/ml) is supplied in 50mM Tris, 300mM NaCl, 10% Glycerol, pH 7.5.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Mesenchymal epithelial transition factor (c-MET) is a proto-oncogenic receptor tyrosine kinase. The endogenous ligand for c-MET is HGF (hepatocyte growth factor), which is a disulfide-linked heterodimeric molecule produced predominantly by mesenchymal cells. In the adult, c-MET protein expression is limited to stem and progenitor cells and is required for wound healing and hepatocyte regeneration. In the embryo, c-MET receptors are expressed on cells of epithelial origin, which are vital for invasive growth and mediate epithelial-mesenchymal transition (EMT). Abnormal activation of the HGF/MET pathway leads to a variety of cancers. c-MET mutation is linked with a poor prognosis since it can trigger tumor growth, angiogenesis and metastasis.

    • Synonyms

      Hepatocyte growth factor receptor, HGF receptor, HGF/SF receptor, Proto-oncogene c-Met, Scatter factor receptor, SF receptor, Tyrosine-protein kinase Met, MET,HGFR, AUTS9, RCCP2.

    • Physical Appearance

      Sterile Filtered clear 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.Please avoid freeze thaw cycles.

    • Amino Acid Sequence

      DSDISSPLLQNTVHIDLSALNPELVQAVQHVVIGPSSLIVHFNEVIGRGHFGCVYHGTL
      LDNDGKKIHCAVKSLNRITDIGEVSQFLTEGIIMKDFSHPNVLSLLGICLRSEGSPLVVL
      PYMKHGDLRNFIRNETHNPTVKDLIGFGLQVAKGMKYLASKKFVHRDLAARNCMLDE
      KFTVKVADFGLARDMYDKEYYSVHNKTGAKLPVKWMALESLQTQKFTTKSDVWSFG
      VLLWELMTRGAPPYPDVNTFDITVYLLQGRRLLQPEYCPDPLYEVMLKCWHPKAEM
      RPSFSELVSRISAIFSTFI.

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    Met Human
  • View Data Sheet

    Name :

    FCGRT Human

    Description:

    Fc Fragment Of IgG Receptor And Transporter Human Recombinant

    IgG receptor FcRn large subunit p51, FcRn, IgG Fc fragment receptor transporter alpha chain, Neonatal Fc receptor, Fcgrt, Fcrn.

    Product # :

    PRO-2806

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    Description

    FCGRT Human Recombinant is a glycosylated, polypeptide chain conteining 2 fragments: FCGRT (24-297aa) having a total 280 a.a and a a molecular weigh of 31.1kDa & B2M (21-119 aa) having a total 99 a.a and a a molecular weigh of 11.7kDa. FCGRT is fused to a 6 a.a his-Tag at C-terminus and is purified by proprietary chromatographic techniques.

    Source

    HEK293 Cells.

    Formulation

    The FCGRT solution (0.25mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Measured by its binding ability in a functional ELISA with Human IgG1 Fc.

    More Info

    • Synonyms

      IgG receptor FcRn large subunit p51, FcRn, IgG Fc fragment receptor transporter alpha chain, Neonatal Fc receptor, Fcgrt, Fcrn.

    • 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

      FCGRT

      AESHLSLLYH LTAVSSPAPG TPAFWVSGWL GPQQYLSYNS LRGEAEPCGA WVWENQVSWY WEKETTDLRI KEKLFLEAFK ALGGKGPYTL QGLLGCELGP DNTSVPTAKF ALNGEEFMNF DLKQGTWGGD WPEALAISQR WQQQDKAANK ELTFLLFSCP HRLREHLERG RGNLEWKEPP SMRLKARPSS PGFSVLTCSA FSFYPPELQL RFLRNGLAAG TGQGDFGPNS DGSFHASSSL TVKSGDEHHY CCIVQHAGLA QPLRVELESP AKSSHHHHHH.

      B2M

      IQRTPKIQVY SRHPAENGKS NFLNCYVSGF HPSDIEVDLL KNGERIEKVE HSDLSFSKDW SFYLLYYTEF TPTEKDEYAC RVNHVTLSQP KIVKWDRDM.

    • Background

      Applications in Drug Delivery and Therapy:

      The unique ability of FCGRT to transport immunoglobulins has spurred investigations into its potential applications in drug delivery. FCGRT Human Recombinant is being explored as a tool to improve the pharmacokinetics of therapeutic antibodies, enhancing their stability and extending their half-life in circulation. This holds significant implications for the development of antibody-based therapies for a range of diseases, including autoimmune disorders and cancer.

      Modulation of Immune Responses:

      Beyond its role in immunoglobulin transport, FCGRT is implicated in the modulation of immune responses. FCGRT Human Recombinant studies have unveiled its interactions with immune cells and its potential influence on the activation and regulation of the immune system. This dual role positions FCGRT as a key player not only in passive immunity but also in the dynamic orchestration of immune responses.

      Challenges and Future Directions:

      While the potential of FCGRT Human Recombinant in drug delivery is promising, challenges persist. Fine-tuning its applications, understanding its interactions with diverse antibodies, and optimizing strategies for therapeutic use are critical considerations for translational success. Additionally, deciphering the intricate balance between immunoglobulin transport and immune modulation is an active area of investigation.

      FCGRT Human Recombinant emerges as a sentinel in the realm of immunoglobulin transport and drug delivery, offering a controlled platform for scientific exploration. Its structural insights, immunoglobulin transport functions, and therapeutic applications position it as a key player in the evolving landscape of biopharmaceuticals. As researchers continue to delve into the molecular intricacies of FCGRT, they not only enhance our understanding of immunoglobulin transport but also pave the way for transformative advancements in drug delivery and antibody-based therapies, shaping the future of precision medicine and targeted therapeutics.

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    Fcgrt Human
  • View Data Sheet

    Name :

    Protein-L, His

    Description:

    Protein L Recombinant, His Tag

    Product # :

    PRO-1930

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    Description

    Recombinant Protein-L produced in E.Coli is a single non-glycosylated polypeptide chain fused with a 6×His tag at N-terminus. Protein-L is comprised of 5 IgG-binding regions of protein L (B1-B2-B3-B4-B5) containing 372 amino acids in total and having a molecular mass of 41.5kDa, however, it migrates with an apparent molecular mass of 46kDa on SDS-PAGE. Cell wall binding region, cell membrane binding region and albumin binding region have been eliminated from the recombinant Protein-L to guarantee the maximum specific IgG binding.

    Source

    Escherichia Coli.

    Formulation

    Protein-L was lyophilized without any additives.

    Purity

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

    More Info

    • Introduction

      The Recombinant Protein L is comprised of 5 kappa-binding domains. Protein L has the exceptional ability to bind through kappa light chain interactions without hindering with the antibody’s antigen-binding site. This gives Protein L the capacity to bind a broader range of Ig classes and subclasses than other antibody-binding proteins. The recombinant Protein L is perfect for purification of polyclonal or monoclonal IgG antibodies. Protein L binds to IgG from humans, mice, rats and pigs.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Protein-L although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Protein-L 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 Protein-L in sterile 18M-cm H2O not less than 0.1mg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MHHHHHHKEE TPETPETDSE EEVTIKANLI FANGSTQTAE FKGTFEKATS EAYAYADTLK KDNGEYTVDV ADKGYTLNIK FAGKEKTPEE PKEEVTIKAN LIYADGKTQT AEFKGTFEEA TAEAYRYADA LKKDNGEYTV DVADKGYTLN IKFAGKEKTP EEPKEEVTIK ANLIYADGKT QTAEFKGTFE EATAEAYRYA DLLAKENGKY TVDVADKGYT LNIKFAGKEK TPEEPKEEVT IKANLIYADG KTQTAEFKGT FAEATAEAYR YADLLAKENG KYTADLEDGG YTINIRFAGK KVDEKPEEKE QVTIKENIYF EDGTVQTATF KGTFAEATAE AYRYADLLSK EHGKYTADLE DGGYTINIRF AG.

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    Protein L His
  • View Data Sheet

    Name :

    COMP Human

    Description:

    Cartilage Oligomeric Matrix Protein Human Recombinant

    Cartilage Oligomeric Matrix Protein (pseudoachondroplasia epiphyseal dysplasia 1 multiple), MED, THBS5, TSP5, EDM1, PSACH, EPD1, Thrombospondin-5

    Product # :

    PRO-2727

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    Description

    COMP Human Recombinant produced in HEK293 Cells is a single, glycosylated polypeptide chain containing 749 amino acids (21-757a.a) and having a molecular mass of 82.4kDa.COMP is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    HEK293 Cells.

    Formulation

    The COMP solution (0. 5mg/1ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      COMP is a non-collagenous glycoprotein and is belongs to the thrombospondin family of extracellular proteins. COMP is a calcium-binding protein of high molecular weight (>500kDa) found in the extracellular matrix of articular, nasal and tracheal cartilage. COMP is not only cartilage-derived but is common in other tissues, such as synovium and tendon. Intact COMP is pentameric, with 5 equal subunits and the carboxy-terminal globular domain of native COMP binds to collagens I, II, and IX. COMP molecules are vital for conserving the properties and integrity of collagen network. Moreover, COMP has a storage and delivery function for hydrophobic cellsignaling molecules such as vitamin D. Mutations of the COMP gene cause Pseudoachondroplasia and some forms of multiple epiphyseal dysplasia which implicates that it is vital that COMP develops and functions normally.

    • Synonyms

      Cartilage Oligomeric Matrix Protein (pseudoachondroplasia epiphyseal dysplasia 1 multiple), MED, THBS5, TSP5, EDM1, PSACH, EPD1, Thrombospondin-5

    • 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

      ADPDAHSLWY NFTIIHLPRH GQQWCEVQSQ VDQKNFLSYD CGSDKVLSMG HLEEQLYATD AWGKQLEMLR EVGQRLRLEL ADTELEDFTP SGPLTLQVRM SCECEADGYI RGSWQFSFDG RKFLLFDSNN RKWTVVHAGA RRMKEKWEKD SGLTTFFKMV SMRDCKSWLR DFLMHRKKRL EPTAPPTMAP GLEPKSCDKT HTCPPCPAPE LLGGPSVFLF PPKPKDTLMI SRTPEVTCVV VDVSHEDPEV KFNWYVDGVE VHNAKTKPRE EQYNSTYRVV SVLTVLHQDW LNGKEYKCKV SNKALPAPIE KTISKAKGQP REPQVYTLPP SRDELTKNQV SLTCLVKGFY PSDIAVEWES NGQPENNYKT TPPVLDSDGS FFLYSKLTVD KSRWQQGNVF SCSVMHEALH NHYTQKSLSL SPGKHHHHHH

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    Comp Protein
  • View Data Sheet

    Name :

    AIDA Human

    Description:

    Axin Interactor Dorsalization Associated Human Recombinant

    C1orf80, RP11-378J18.7, Axin interactor, dorsalization-associated protein, Axin interaction partner and dorsalization antagonist, AIDA.

    Product # :

    PRO-1370

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    Description

    AIDA Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 329 amino acids (1-306 a.a) and having a molecular mass of 37.4kDa. AIDA is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    AIDA protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 0.2M NaCl and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Axin interactor, dorsalization-associated (AIDA) operates as a ventralizing factor during embryogenesis. AIDA inhibits axin-mediated JNK activation by binding axin and disrupting axin homodimerization. That in turn antagonizes a Wnt/beta-catenin-independent dorsalization pathway activated by AXIN/JNK-signaling.

    • Synonyms

      C1orf80, RP11-378J18.7, Axin interactor, dorsalization-associated protein, Axin interaction partner and dorsalization antagonist, AIDA.

    • 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 MGSMSEVTRS LLQRWGASFR RGADFDSWGQ LVEAIDEYQI LARHLQKEAQ AQHNNSEFTE EQKKTIGKIA TCLELRSAAL QSTQSQEEFK LEDLKKLEPI LKNILTYNKE FPFDVQPVPL RRILAPGEEE NLEFEEDEEE GGAGAGSPDS FPARVPGTLL PRLPSEPGMT LLTIRIEKIG LKDAGQCIDP YITVSVKDLN GIDLTPVQDT PVASRKEDTY VHFNVDIELQ KHVEKLTKGA AIFFEFKHYK PKKRFTSTKC FAFMEMDEIK PGPIVIELYK KPTDFKRKKL QLLTKKPLYL HLHQTLHKE.

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    Aida Human
  • View Data Sheet

    Name :

    IMPAD1 Mouse Bioactive

    Description:

    Inositol Monophosphatase Domain Containing 1 Mouse Recombinant Bioactive

    Inositol monophosphatase 3, IMP 3, IMPase 3, Golgi 3-prime phosphoadenosine 5-prime phosphate 3-prime phosphatase, Golgi-resident PAP phosphatase, gPAPP, Inositol monophosphatase domain-containing protein 1, Inositol-1(or 4)-monophosphatase 3, Myo-inositol monophosphatase A3.

    Product # :

    PRO-2380

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    Description

    IMPAD1 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 332 amino acids (34-356a.a.) and having a molecular mass of 36.2kDa. (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). IMPAD1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    IMPAD1 protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 5,000 pmol/min/ug and is defined as the amount of enzyme that hydrolyze Adenosine 3, 5-diphosphate per minute at pH 7.5 at 25C.

    More Info

    • Introduction

      Inositol monophosphatase 3 (IMPAD1) belongs to the inositol monophosphatase family. IMPAD1 is restricted to the Golgi apparatus and catalyzes the hydrolysis of phosphoadenosine phosphate (PAP) to adenosine monophosphate (AMP). IMPAD1 gene mutations cause the GRAPP type chondrodysplasia with joint dislocations, and a pseudogene of the IMPAD1 gene is located on the long arm of chromosome 1.

    • Synonyms

      Inositol monophosphatase 3, IMP 3, IMPase 3, Golgi 3-prime phosphoadenosine 5-prime phosphate 3-prime phosphatase, Golgi-resident PAP phosphatase, gPAPP, Inositol monophosphatase domain-containing protein 1, Inositol-1(or 4)-monophosphatase 3, Myo-inositol monophosphatase A3.

    • 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

      ADPGRFSLFG LGSEPAAGEA EVASDGGTVD LREMLAVAVL AAERGGDEVR RVRESNVLHE KSKGKTREGA DDKMTSGDVL SNRKMFYLLK TAFPNVQINT EEHVDASDKE VIVWNRKIPE DILKEIAAPK EVPAESVTVW IDPLDATQEY TEDLRKYVTT MVCVAVNGKP VLGVIHKPFS EYTAWAMVDG GSNVKARSSY NEKTPKIIVS RSHAGMVKQV ALQTFGNQTS IIPAGGAGYK VLALLDVPDM TQEKADLYIH VTYIKKWDIC AGNAILKALG GHMTTLNGEE ISYTGSDGIE GGLLASIRMN HQALVRKLPD LEKSGHHHHH HH.

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

    Impad1 Mouse Bioactive
  • View Data Sheet

    Name :

    GINS4 Human

    Description:

    GINS Complex Subunit 4 Protein Human Recombinant

    SLD5, GINS complex subunit 4, DNA replication complex GINS protein SLD5.

    Product # :

    PRO-1270

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    Description

    GINS4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 243 amino acids (1-223 a.a.) and having a molecular mass of 28.2kDa.GINS4 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GINS4 protein solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl,20% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      GINS4, a member of the GINS4/SLD5 family, has a key part in the initiation of DNA replication, and progression of DNA replication forks. GINS4 is significant for GINS complex assembly. GINS complex connects favorably to singlestranded DNA. Recombinant human GINS4 protein, fused to His-tag at N-terminus was purified by using conventional chromatography techniques.

    • Synonyms

      SLD5, GINS complex subunit 4, DNA replication complex GINS protein SLD5.

    • 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 MTEEVDFLGQ DSDGGSEEVV LTPAELIERL EQAWMNEKFA PELLESKPEI VECVMEQLEH MEENLRRAKR EDLKVSIHQM EMERIRYVLS SYLRCRLMKI EKFFPHVLEK EKTRPEGEPS SLSPEELAFA REFMANTESY LKNVALKHMP PNLQKVDLFR AVPKPDLDSY VFLRVRERQE NILVEPDTDE QRDYVIDLEK GSQHLIRYKT IAPLVASGAV QLI

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    Gins4 Human
  • View Data Sheet

    Name :

    RPS24 Human

    Description:

    Ribosomal Protein S24 Human Recombinant

    Ribosomal Protein S24, 40S Ribosomal Protein S24, DBA3, S24.

    Product # :

    PRO-1554

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    Description

    RPS24 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 153 amino acids (1-130) and having a molecular mass of 17.5kDa.RPS24 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The RPS24 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 2mM DTT and 50% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      RPS24 is a member of the S24E family of ribosomal proteins. RPS24 is situated in the cytoplasm. Numerous transcript variations encoding different isoforms were identified for this gene. There are multiple processed pseudogenes of this gene distributed all over the genome just like other genes encoding ribosomal proteins. Alterations in RPS24 cause Diamond-Blackfan anemia.

    • Synonyms

      Ribosomal Protein S24, 40S Ribosomal Protein S24, DBA3, S24.

    • 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 MGSMNDTVTI RTRKFMTNRL LQRKQMVIDV LHPGKATVPK TEIREKLAKM YKTTPDVIFV FGFRTHFGGG KTTGFGMIYD SLDYAKKNEP KHRLARHGLY EKKKTSRKQR KERKNRMKKV RGTAKANVGA GKK

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    Rps24 Human
  • View Data Sheet

    Name :

    EPO Mouse

    Description:

    Erythropoietin Mouse Recombinant

    Erythropoietin, erythropoietin isoform 1 precursor, Epo.

    Product # :

    CYT-1171

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    • sds-page

    Description

    EPO Mouse Recombinant produced in Baculovirus is a single glycosylated polypeptide chain containing 176 amino acids (27-192 aa) and having a molecular mass of 19.8kDa.EPO is fused to a 9 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    EPO Mouse protein (0.25mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Measured in a cell proliferation assay using TF-1 human erythroleukemic cells. The ED50 range ≤ 2ng/ml.

    sds-page

    EPO-sds-page - Product image 1

    More Info

    • Introduction

      Erythropoietin or EPO is a hormone (glycoprotein), part of the type I cytokine group of proteins. EPO is found mainly in the kidney tissue, produced from fibroblast-like cortical interstitial cells near the proximal tubules. EPO is also present in the blood, where it acts as red cell production regulator, by the promotion of differentiation of erythroid and thereby starts hemoglobin synthesis. Furthermore, EPO has neuroprotective activity towards brain injuries & anti-apoptotic activity in different tissues.

    • Synonyms

      Erythropoietin, erythropoietin isoform 1 precursor, Epo.

    • 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

      ADPMAPPRLI CDSRVLERYI LEAKEAENVT MGCAEGPRLS ENITVPDTKV NFYAWKRMEV EEQAIEVWQG LSLLSEAILQ AQALLANSSQ PPETLQLHID KAISGLRSLT SLLRVLGAQK ELMSPPDTTP PAPLRTLTVD TFCKLFRVYA NFLRGKLKLY TGEVCRRGDR HHHHHH.

    • Background

      What is the molecular weight/Mw of EPO Protein?
      EPO Protein has a total Mw of 19.8kDa.

      What is the source or expression system of EPO Protein?
      Sf9, Baculovirus cells.

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

      What is the Biological Activity of EPO Protein?
      Measured in a cell proliferation assay using TF-1 human erythroleukemic cells. The ED50 range ≤ 2ng/ml.

      What is the amino acid sequence of EPO Protein?
      ADPMAPPRLI CDSRVLERYI LEAKEAENVT MGCAEGPRLS ENITVPDTKV NFYAWKRMEV EEQAIEVWQG LSLLSEAILQ AQALLANSSQ PPETLQLHID KAISGLRSLT SLLRVLGAQK ELMSPPDTTP PAPLRTLTVD TFCKLFRVYA NFLRGKLKLY TGEVCRRGDR HHHHHH.

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

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

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