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Search results

1000 results found for “Calcium Binding Protein”

Name

Description

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  • View Data Sheet

    Name :

    DNAJC27 Human

    Description:

    DnaJ (Hsp40) Homolog, Subfamily C, Member 27 Human Recombinant

    DnaJ homolog subfamily C member 27, DnaJ (Hsp40) Homolog, Subfamily C, Member 27, DNAJC27, Rab and DnaJ domain-containing protein, RABJS, RBJ, dnaJ homolog subfamily C member 27 isoform 1.

    Product # :

    HSP-060

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    Description

    DNAJC27 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 296 amino acids (1-273 a.a.) and having a molecular mass of 33.2kDa. DNAJC27 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The DNAJC27 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 50% glycerol, 2mM DTT and 2mM EDTA.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      DnaJ (Hsp40) Homolog, Subfamily C, Member 27 (DNAJC27) which contains one J domain is a part of the small GTPase superfamily. DNAJC27 is a GTPase which activates the MEK/ERK pathway and induces cell transformation when overexpressed.

    • Synonyms

      DnaJ homolog subfamily C member 27, DnaJ (Hsp40) Homolog, Subfamily C, Member 27, DNAJC27, Rab and DnaJ domain-containing protein, RABJS, RBJ, dnaJ homolog subfamily C member 27 isoform 1.

    • 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 MGSMEANMPK RKEPGRSLRI KVISMGNAEV GKSCIIKRYC EKRFVSKYLA TIGIDYGVTK VHVRDREIKV NIFDMAGHPF FYEVRNEFYK DTQGVILVYD VGQKDSFDAL DAWLAEMKQE LGPHGNMENI IFVVCANKID CTKHRCVDES EGRLWAESKG FLYFETSAQT GEGINEMFQT FYISIVDLCE NGGKRPTTNS SASFTKEQAD AIRRIRNSKD SWDMLGVKPG ASRDEVNKAY RKLAVLLHPD KCVAPGSEDA FKAVVNARTA LLKNIK.

    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.

    Dnajc27 Human
  • View Data Sheet

    Name :

    COPS7A Human

    Description:

    COP9 Signalosome Subunit 7A Human Recombinant

    COP9 Signalosome Subunit 7A, COPS7A, Dermal Papilla-Derived Protein 10, CSN7A, SGN7a, JAB1-Containing Signalosome Subunit 7a, COP9 Complex Subunit 7a, COP9 Constitutive Photomorphogenic Homolog Subunit 7A, COP9 Signalosome Complex Subunit 7a, DERP10, Signalosome Subunit 7a.

    Product # :

    PRO-1947

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    Description

    COPS7A Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 298 amino acids (1-275) and having a molecular mass of 32.7 kDa.COPS7A is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The COPS7A solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      COP9 Signalosome Subunit 7A (COPS7A) is a component of the COP9 signalosome complex (CSN), a complex involved in a variety of cellular and developmental processes. The CSN complex is a vital regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes, thus leading to decrease in the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2. This complex is also involved in phosphorylation of p53/TP53, JUN, I-kappa-B-alpha/NFKBIA, ITPK1 and IRF8/ICSBP, probably through its association with CK2 and PKD kinases. CSN-dependent phosphorylation of TP53 and JUN stimulates and protects degradation by the Ubl system, respectively.

    • Synonyms

      COP9 Signalosome Subunit 7A, COPS7A, Dermal Papilla-Derived Protein 10, CSN7A, SGN7a, JAB1-Containing Signalosome Subunit 7a, COP9 Complex Subunit 7a, COP9 Constitutive Photomorphogenic Homolog Subunit 7A, COP9 Signalosome Complex Subunit 7a, DERP10, Signalosome Subunit 7a.

    • 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 MGSMSAEVKV TGQNQEQFLL LAKSAKGAAL ATLIHQVLEA PGVYVFGELL DMPNVRELAE SDFASTFRLL TVFAYGTYAD YLAEARNLPP LTEAQKNKLR HLSVVTLAAK VKCIPYAVLL EALALRNVRQ LEDLVIEAVY ADVLRGSLDQ RNQRLEVDYS IGRDIQRQDL SAIARTLQEW CVGCEVVLSG IEEQVSRANQ HKEQQLGLKQ QIESEVANLK KTIKVTTAAA AAATSQDPEQ HLTELREPAP GTNQRQPSKK ASKGKGLRGS AKIWSKSN.

    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.

    Cops7A Human
  • View Data Sheet

    Name :

    CXCL5 Human (8-78 a.a)

    Description:

    Epithelial Neutrophil-Activating Protein 78, 8-78 a.a. Human Recombinant (CXCL5)

    Small inducible cytokine B5, CXCL5, Epithelial-derived neutrophil-activating protein 78, Neutrophil-activating peptide ENA-78, ENA-78(1-78), chemokine (C-X-C motif) ligand 5, SCYB5.

    Product # :

    CHM-265

    Price :

    Quantity :

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    • description
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    Description

    Epithelial Neutrophil-Activating Protein 78 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 71 amino acids (8-78 a.a.) and having a molecular mass of 7.8kDa. The CXCL5 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in 1xPBS, pH 7.4.

    Purity

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

    Biological Activity

    The biological activity was determined by its ability to chemoattract human peripheral blood neutrophils using a concentration range of 10.0-100.0 ng/ml.

    More Info

    • Introduction

      Chemokine (C-X-C motif) ligand 5 (CXCL5) is a small cytokine belonging to the CXC chemokine family that is also known as epithelial-derived neutrophil-activating peptide 78 (ENA-78). It is produced following stimulation of cells with the inflammatory cytokines interleukin-1 or tumor necrosis factor-alpha. Expression of CXCL5 has also been observed in eosinophils, and can be inhibited with the type II interferon IFN-?. This chemokine stimulates the chemotaxis of neutrophils possesses angiogenic properties. It elicits these effects by interacting with the cell surface chemokine receptor CXCR2. The gene for CXCL5 is encoded on four exons and is located on human chromosome 4 amongst several other CXC chemokine genes. CXCL5 has been implicated in connective tissue remodelling.

    • Synonyms

      Small inducible cytokine B5, CXCL5, Epithelial-derived neutrophil-activating protein 78, Neutrophil-activating peptide ENA-78, ENA-78(1-78), chemokine (C-X-C motif) ligand 5, SCYB5.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized ENA78 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL5 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 ENA-78 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      LRELRCVCLQ TTQGVHPKMI SNLQVFAIGP QCSKVEVVAS LKNGKEICLD PEAPFLKKVI QKILDGGNKE N.

    • Background

      What is the molecular weight/Mw of CXCL5 HUMAN (8-78 A.A) Protein?
      CXCL5 HUMAN (8-78 A.A) Protein has a total Mw of 7.8kDa.

      What is the source or expression system of CXCL5 HUMAN (8-78 A.A) Protein?
      Escherichia Coli.

      What is the Purity of CXCL5 HUMAN (8-78 A.A) Protein?
      CXCL5 HUMAN (8-78 A.A) Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL5 HUMAN (8-78 A.A) Protein?
      The biological activity was determined by its ability to chemoattract human peripheral blood neutrophils using a concentration range of 10.0-100.0 ng/ml.

      What is the amino acid sequence of CXCL5 HUMAN (8-78 A.A) Protein?
      LRELRCVCLQ TTQGVHPKMI SNLQVFAIGP QCSKVEVVAS LKNGKEICLD PEAPFLKKVI QKILDGGNKE N.

      What applications can CXCL5 HUMAN (8-78 A.A) Protein be used in?
      CXCL5 HUMAN (8-78 A.A) Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL5 HUMAN (8-78 A.A) Protein?
      The endotoxin level is minimal, CXCL5 HUMAN (8-78 A.A) 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.

    Ena 78 Human 8 78 Aa
  • View Data Sheet

    Name :

    HRSP12 Human

    Description:

    Heat-Responsive Protein 12 Human Recombinant

    Ribonuclease UK114, 14.5 kDa translational inhibitor protein, p14.5, Heat-responsive protein 12, UK114 antigen homolog, HRSP12, PSP.

    Product # :

    PRO-052

    Price :

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    Description

    HRSP12 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 157 amino acids (1-137 a.a.) and having a molecular mass of 16.6kDa. The HRSP12 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The HRSP12 solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 0.1M NaCl and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      HRSP12 (UK114) is an endoribonuclease found mainly in the human adult kidney and liver, and which is responsible for inhibiting translation by cleaving mRNA. HRSP12 cleaves phosphodiester bonds only in single-stranded RNA. HRSP12 may be an important biomarker for heptatic carcinoma.

    • Synonyms

      Ribonuclease UK114, 14.5 kDa translational inhibitor protein, p14.5, Heat-responsive protein 12, UK114 antigen homolog, HRSP12, PSP.

    • 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 MSSLIRRVIS TAKAPGAIGP YSQAVLVDRT IYISGQIGMD PSSGQLVSGG VAEEAKQALK NMGEILKAAG CDFTNVVKTT VLLADINDFN TVNEIYKQYF KSNFPARAAY QVAALPKGSR IEIEAVAIQG PLTTASL.

    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.

    Hrsp12 Human
  • View Data Sheet

    Name :

    CLIC2 Human

    Description:

    Chloride Intracellular Channel 2 Human Recombinant

    Chloride intracellular channel protein 2, XAP121, CLIC2, CLIC2b, XAP121.

    Product # :

    PRO-198

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    Description

    CLIC2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 267 amino acids (1-247 a.a.) and having a molecular mass of 30.5kDa.CLIC2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CLIC2 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol 0.1M NaCl and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Chloride intracellular channel protein 2 (CLIC2) regulates cellular traffic of chloride ions, which is a critical component of all living cells. CLIC2 is involved in membrane potential stabilization, signal transduction, cell volume regulation and organic solute transport. CLIC2 is identified in the fetal liver and adult skeletal muscle tissue. CLIC2 is a likely candidate for one of the many diseases linked to Xq28.

    • Synonyms

      Chloride intracellular channel protein 2, XAP121, CLIC2, CLIC2b, XAP121.

    • 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 MSGLRPGTQV DPEIELFVKA GSDGESIGNC PFCQRLFMIL WLKGVKFNVT TVDMTRKPEE LKDLAPGTNP PFLVYNKELK TDFIKIEEFL EQTLAPPRYP HLSPKYKESF DVGCNLFAKF SAYIKNTQKE ANKNFEKSLL KEFKRLDDYL NTPLLDEIDP
      DSAEEPPVSR RLFLDGDQLT LADCSLLPKL NIIKVAAKKY RDFDIPAEFS GVWRYLHNAY AREEFTHTCP EDKEIENTYA NVAKQKS.

    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.

    Clic2 Human
  • View Data Sheet

    Name :

    BLyS Human

    Description:

    B-cell Activating Factor Human Recombinant

    BAFF, BLYS, CD257, TALL1, THANK, ZTNF4, TALL-1, TNFSF20, TNFSF13B, B-cell Activating Factor.

    Product # :

    CYT-307

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    Description

    BAFF Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 153 amino acids and having a molecular mass of 17007 Dalton. The BAFF is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.0.

    Purity

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

    Biological Activity

    The activity is determined by a mouse splenocyte survival assay. The ED50 for this effect is 0.5-2.0µg/ml.

    More Info

    • Introduction

      BAFF binds to tnfrsf13b/taci and tnfrsf17/bcma. Tnfsf13/april binds to the same 2 receptors, together, they form a 2 ligands -2 receptors pathway involved in the stimulation of b- and t-cell function and the regulation of humoral immunity. A third b-cell specific baff-receptor (baffr/br3) promotes the survival of mature b-cells and the b-cell response.
      B Lymphocyte Stimulator functions as a potent B-cell growth factor in costimulation assays.
      Administration of BAFF Human recombinant to mice disrupts splenic B-cell and T-cell zones and results in elevated levels of serum immunoglobulin.

    • Synonyms

      BAFF, BLYS, CD257, TALL1, THANK, ZTNF4, TALL-1, TNFSF20, TNFSF13B, B-cell Activating Factor.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MAVQGPEETV TQDCLQLIAD SETPTIQKGS YTFVPWLLSF KRGSALEEKE NKILVKETGY FFIYGQVLYT DKTYAMGHLI QRKKVHVFGD ELSLVTLFRC IQNMPETLPN NSCYSAGIAK LEEGDELQLA IPRENAQISL DGDVTFFGAL KLL.

    • Background

      What is the molecular weight/Mw of BLYS Protein?
      BLYS Protein has a total Mw of 17.7kDa.

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

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

      What is the Biological Activity of BLYS Protein?
      The activity is determined by a mouse splenocyte survival assay. The ED50 for this effect is 0.5-2.0µg/ml.

      What is the amino acid sequence of BLYS Protein?
      MAVQGPEETV TQDCLQLIAD SETPTIQKGS YTFVPWLLSF KRGSALEEKE NKILVKETGY FFIYGQVLYT DKTYAMGHLI QRKKVHVFGD ELSLVTLFRC IQNMPETLPN NSCYSAGIAK LEEGDELQLA IPRENAQISL DGDVTFFGAL KLL.

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

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

    Blys Human
  • View Data Sheet

    Name :

    SIRPB1 Human

    Description:

    Recombinant Human Signal Regulatory Protein Beta 1

    SIRPB1, CD172b, SIRP-BETA-1, SIRP-Beta-1 Isoform 3, CD172b Antigen, CD172b.

    Product # :

    PRO-2545

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    Description

    SIRPB1produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (30-371 a.a.) and fused to a 6 aa His Tag at C-terminus containing a total of 348 amino acids and having a molecular mass of 38.0kDa. SIRPB1shows multiple bands between 40-57kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    SIRPB1protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) & 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Signal-regulatory protein beta-1 isoform 1 or SIRPB1, is an immunoglobulin-like cell surface receptor which is a part of the SIRP superfamily. SIRPB1 is a cell membrane receptor that takes part in the negative regulation of tyrosine kinase-coupled signaling pathway. SIRPB1 is engaged in the activation of tyrosine kinase SYK, SIRP alpha molecules (activates SHP-1 and SHP-2 protein tyrosine phosphatases), etc.

    • Synonyms

      SIRPB1, CD172b, SIRP-BETA-1, SIRP-Beta-1 Isoform 3, CD172b Antigen, CD172b.

    • 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

      EDELQVIQPE KSVSVAAGES ATLRCAMTSL IPVGPIMWFR GAGAGRELIY NQKEGHFPRV TTVSELTKRN NLDFSISISN ITPADAGTYY CVKFRKGSPD DVEFKSGAGT ELSVRAKPSA PVVSGPAVRA TPEHTVSFTC ESHGFSPRDI TLKWFKNGNE LSDFQTNVDP AGDSVSYSIH STARVVLTRG DVHSQVICEI AHITLQGDPL RGTANLSEAI RVPPTLEVTQ QPMRAENQAN VTCQVSNFYP RGLQLTWLEN GNVSRTETAS TLIENKDGTY NWMSWLLVNT CAHRDDVVLT CQVEHDGQQA VSKSYALEIS AHQKEHGSDI THEAALAPTA PLHHHHHH.

    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.

    Sirpb1 Human
  • View Data Sheet

    Name :

    Protein-A/G, His

    Description:

    Protein A/G Recombinant, His Tag

    Product # :

    PRO-1927

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    Description

    Protein-A/G Recombinant produced in E.Coli is a single non-glycosylated polypeptide chain fused with a 6×His tag at C-terminus. Protein-A/G is comprised of 5 IgG-binding regions of protein A (E-D-A-B-C) and 3 of protein G (C1-C2-C3) containing 513 amino acids in total and having a molecular mass of 56.9kDa. Cell wall binding region, cell membrane binding region and albumin binding region have been eliminated from the recombinant Protein A/G to guarantee the maximum specific IgG binding.

    Source

    Escherichia Coli.

    Formulation

    Protein-A/G was lyophilized without any additives.

    Purity

    Greater than 96.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    More Info

    • Introduction

      The recombinant Protein A/G is a genetically engineered protein comprised of 8 IgG-binding domains EDABC-C1C2C3, corresponding to the Protein A and G domains which are included in the recombinant sequence. The Protein A part is from Staphylococcus aureus segments E, D, A, B and C. The Protein G part is from Streptococcus segments C1, C2 and C3. The recombinant Protein A/G has a broader binding capacity than either Protein A or Protein G alone. The recombinant Protein A/G is ideal for purification of monoclonal or polyclonal IgG antibodies. Protein A/G binds to various human, mouse and rat IgG subclasses such as the human IgG1, IgG2, IgG3, IgG4; mouse IgG2a, IgG2b, IgG3 and rat IgG2a, IgG2c. In addition, Protein A/G binds to total IgG from cow, goat, sheep, horse, rabbit, guinea pig, pig, dog and cat.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MNAAQHDEAQ QNAFYQVLNM PNLNADQRNG FIQSLKDDPS QSANVLGEAQ KLNDSQAPKA DAQQNNFNKD QQSAFYEILN MPNLNEAQRN GFIQSLKDDP SQSTNVLGEA KKLNESQAPK ADNNFNKEQQ NAFYEILNMP NLNEEQRNGF IQSLKDDPSQ SANLLSEAKK LNESQAPKAD NKFNKEQQNA FYEILHLPNL NEEQRNGFIQ SLKDDPSQSA NLLAEAKKLN DAQAPKADNK FNKEQQNAFY EILHLPNLTE EQRNGFIQSL KDDPSVSKEI LAEAKKLNDA QAPKEEDSLE GSGSGTYKLI LNGKTLKGET TTEAVDAATA EKVFKQYAND NGVDGEWTYD DATKTFTVTE KPEVIDASEL TPAVTTYKLV INGKTLKGET TTEAVDAATA EKVFKQYAND NGVDGEWTYD DATKTFTVTE KPEVIDASEL TPAVTTYKLV INGKTLKGET TTKAVDAETA EKAFKQYAND NGVDGVWTYD DATKTFTVTE KLAAALEHHH HHH.

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

    Protein A G His
  • View Data Sheet

    Name :

    TFRC Native

    Description:

    Transferrin Receptor Human

    Transferrin receptor protein 1, TR, TfR, TfR1, Trfr, T9, p90, CD_antigen: CD71, Transferrin receptor, serum form, sTfR, TFRC, CD71

    Product # :

    PRO-2742

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    Description

    Human Transferrin Receptor Protein produced in human serum tissue having a molecular mass of 85kDa.

    Source

    Human serum.

    Formulation

    TFRC Native solution (0.2µm filtered) contains 250mM TRIS-HCl buffer, 0.15M NaCl, 0.09% NaN3, pH 8.0.

    More Info

    • Introduction

      Transferrin receptor protein 1 (TFRC) is required for iron delivery from transferring to cells. The TFRC protein is a transmembrane glycoprotein comprised of 2 disulfide-linked monomers joined by 2 disulfide bonds. Each monomer will bind one holo-transferrin molecule producing an iron-Tf-TfR complex which enters the cell by endocytosis.

    • Synonyms

      Transferrin receptor protein 1, TR, TfR, TfR1, Trfr, T9, p90, CD_antigen: CD71, Transferrin receptor, serum form, sTfR, TFRC, CD71

    • Physical Appearance

      Sterile Filtered brown 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.

    • Human Virus Test

      Starting material donor has been tested and certified negative for antibodies to HIV-1, HIV-2, HCV, HBSAG, Parvovirus B19, Syphilis and HIV/HBV/HCV (PCR).

    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.

    Transferrin Receptor Tfrc
  • View Data Sheet

    Name :

    Protein Cys-A/G

    Description:

    Protein Cys-A/G Recombinant

    Product # :

    PRO-1929

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    Description

    Protein-A/G Recombinant produced in E.Coli is a single non-glycosylated polypeptide chain fused with a Cys at N-terminus. Protein-A/G is comprised of 5 IgG-binding regions of protein A (E-D-A-B-C) and 2 of protein G (C1-C3) containing 430 amino acids in total and having a molecular mass of 47.8kDa. Cell wall binding region, cell membrane binding region and albumin binding region have been eliminated from the recombinant Protein A/G to guarantee the maximum specific IgG binding.

    Source

    Escherichia Coli.

    Formulation

    Protein-A/G was lyophilized without any additives.

    Purity

    Greater than 96.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    More Info

    • Introduction

      The recombinant Protein A/G is a genetically engineered protein comprised of 7 IgG-binding domains EDABC-C1C3, corresponding to the Protein A and G domains which are included in the recombinant sequence. The Protein A part is from Staphylococcus aureus segments E, D, A, B and C. The Protein G part is from Streptococcus segments C1 and C3. The recombinant Protein A/G has a broader binding capacity than either Protein A or Protein G alone. The recombinant Protein A/G is ideal for purification of monoclonal or polyclonal IgG antibodies. Protein A/G binds to various human, mouse and rat IgG subclasses such as the human IgG1, IgG2, IgG3, IgG4; mouse IgG2a, IgG2b, IgG3 and rat IgG2a, IgG2c. In addition, Protein A/G binds to total IgG from cow, goat, sheep, horse, rabbit, guinea pig, pig, dog and cat.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      CNAAQHDEAQ QNAFYQVLNM PNLNADQRNG FIQSLKDDPS QSANVLGEAQ KLNDSQAPKA DAQQNNFNKD QQSAFYEILN MPNLNEAQRN GFIQSLKDDP SQSTNVLGEA KKLNESQAPK ADNNFNKEQQ NAFYEILNMP NLNEEQRNGF IQSLKDDPSQ SANLLSEAKK LNESQAPKAD NKFNKEQQNA FYEILHLPNL NEEQRNGFIQ SLKDDPSQSA NLLAEAKKLN DAQAPKADNK FNKEQQNAFY EILHLPNLTE EQRNGFIQSL KDDPSVSKEI LAEAKKLNDA QAPKEEDSLE GSGSGTYKLI LNGKTLKGET TTEAVDAATA EKVFKQYAND NGVDGEWTYD DATKTFTVTE KPEVIDASEL TPAVTTYKLV INGKTLKGET TTKAVDAETA EKAFKQYAND NGVDGVWTYD DATKTFTVTE.

    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.

    Protein Cys A G
  • 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.

    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.

    Aida Human
  • View Data Sheet

    Name :

    VPS24 Human

    Description:

    Vacuolar Protein Sorting 24 Human Recombinant

    Charged multivesicular body protein 3, Chromatin-modifying protein 3, Neuroendocrine differentiation factor, Vacuolar protein sorting-associated protein 24, hVps24, CHMP3, CGI149, NEDF, VPS24, CGI-149.

    Product # :

    PRO-872

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    Description

    VPS24 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 242 amino acids (1-222 a.a) and having a molecular mass of 27.2kDa (Molecular weight on SDS-PAGE will appear higher).VPS24 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    VPS24 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Charged multivesicular body protein 3 (VPS24/CHMP3) is a member of the vacuolar sorting protein family and function as chromatin modifying proteins. VPS24 links directly with CHMP2 and CHMP4 for the disassembly of ESCRT-III complex in an ATP-dependent manner. During HIV-1 infection, the virus uses the ESCRT-III complex to mediate budding and exocytosis of viral proteins. VPS24 overexpression strongly hinders HIV-1 release.

    • Synonyms

      Charged multivesicular body protein 3, Chromatin-modifying protein 3, Neuroendocrine differentiation factor, Vacuolar protein sorting-associated protein 24, hVps24, CHMP3, CGI149, NEDF, VPS24, CGI-149.

    • 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 MGLFGKTQEK PPKELVNEWS LKIRKEMRVV DRQIRDIQRE EEKVKRSVKD AAKKGQKDVC IVLAKEMIRS RKAVSKLYAS KAHMNSVLMG MKNQLAVLRV AGSLQKSTEV MKAMQSLVKI PEIQATMREL SKEMMKAGII EEMLEDTFES MDDQEEMEEE AEMEIDRILF EITAGALGKA PSKVTDALPE PEPPGAMAAS EDEEEEEEAL EAMQSRLATL RS.

    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.

    Vps24 Human
  • View Data Sheet

    Name :

    ARL9 Human

    Description:

    ADP-Ribosylation Factor-Like 9 Human Recombinant

    ADP-ribosylation factor-like protein 9, ARL9.

    Product # :

    PRO-1009

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    Description

    ARL9 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 143 amino acids (1-123 a.a.) and having a molecular mass of 15.9kDa. ARL9 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ARL9 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 20% glycerol and 200mM NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      ADP-ribosylation factor-like protein 9 (ARL9) is a member of to 2 novel subfamilies coding for small GTPases that were found to be highly conserved among eukaryotes.

    • Synonyms

      ADP-ribosylation factor-like protein 9, ARL9.

    • 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 MEFLEIGGSK PFRSYWEMYL SKGLLLIFVV DSADHSRLPE AKKYLHQLIA ANPVLPLVVF ANKQDLEAAY HITDIHEALA LSEVGNDRKM FLFGTYLTKN GSEIPSTMQD AKDLIAQLAA DVQ.

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    Arl9 Human
  • View Data Sheet

    Name :

    AKAP7 Human

    Description:

    A Kinase Anchor Protein 7 Human Recombinant

    A kinase (PRKA) anchor protein 7, A-kinase anchor protein 18 kDa, A-kinase anchor protein 9, kDa PRKA7 isoforms alpha/beta, PRKA7 isoform gamma, AKAP15, AKAP18.

    Product # :

    PKA-030

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    • More Info

    Description

    AKAP7 Human Recombinant produced in E. coli is a single polypeptide chain containing 105 amino acids (1-81) and having a molecular mass of 11.5kDa.AKAP7 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The AKAP7 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 50mM NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      AKAP7 is a member of the A-kinase anchoring protein (AKAP) family, a group of functionally related proteins which bind to a regulatory subunit (RII) of cAMP-dependent protein kinase A (PKA) and target the enzyme to specific subcellular sections. AKAP7 is expressed in heart, brain, pancreas, lung and skeletal muscle. AKAP7 binds PKA to the plasma membrane, and allows efficient coupling to the L-type calcium channel.

    • Synonyms

      A kinase (PRKA) anchor protein 7, A-kinase anchor protein 18 kDa, A-kinase anchor protein 9, kDa PRKA7 isoforms alpha/beta, PRKA7 isoform gamma, AKAP15, AKAP18.

    • 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 MGSHMGQLCC FPFSRDEGKI SEKNGGEPDD AELVRLSKRL VENAVLKAVQ QYLEETQNKN KPGEGSSVKT EAADQNGNDN ENNRK

    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.

    Akap7 Human
  • View Data Sheet

    Name :

    BMP 5 Human

    Description:

    Bone Morphogenetic protein-5 Human Recombinant

    Bone morphogenetic protein 5, BMP-5, BMP5, MGC34244.

    Product # :

    CYT-660

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    • sds-page

    Description

    BMP-5 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 139 amino acids (317-454 a.a.) and having a total molecular mass of 15.7 kDa.BMP-5 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The BMP-5 solution contains 10mM Sodium Citrate buffer (pH3.5) and 10% Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    sds-page

    BMP5-sds-page - Product image 1

    More Info

    • Introduction

      BMP5 belongs to the bone morphogenetic protein family which is part of the transforming growth factor-beta superfamily. This superfamily is comprised of large families of growth and differentiation factors. Bone morphogenetic proteins were initially identified by their ability of demineralizing bone extract to induce endochondral osteogenesis in vivo in an extraskeletal site.
      BMP5 is an essential signaling molecule within the trabecular meshwork and optic nerve head, and may play a potential role in glaucoma pathogenesis. It was shown that BMP-5 increases the levels of osteopontin, BMP-2, alkaline phosphatase and core binding factor alpha 1 mRNAs in human periodontal (HPL) ligament cells. The BMP5 protein is expressed in normal synovial tissue and reduced in osteoarthritis and rheumatoid arthritis. BMP5 may have a role in certain cancers given that it is differentially regulated during the formation of different tumors.

    • Synonyms

      Bone morphogenetic protein 5, BMP-5, BMP5, MGC34244.

    • 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

      MAANKRKNQN RNKSSSHQDS SRMSSVGDYN TSEQKQACKK HELYVSFRDL GWQDWIIAPE GYAAFYCDGE CSFPLNAHMN ATNHAIVQTL VHLMFPDHVP KPCCAPTKLN AISVLYFDDS SNVILKKYRN MVVRSCGCH.

    • Background

      Bone Morphogenetic Protein-5 Human Recombinant: Unleashing the Potential for Tissue Engineering and Regenerative Medicine

      Abstract:

      Bone Morphogenetic Protein-5 (BMP-5) human recombinant is a pivotal member of the bone morphogenetic protein family, known for its crucial role in tissue development, repair, and regeneration. This research paper provides an in-depth analysis of BMP-5, including its characteristics, signaling pathways, and potential therapeutic applications. Additionally, innovative methodologies for the production and optimization of BMP-5 human recombinant are proposed, shedding light on its future implications in the field of tissue engineering and regenerative medicine.

      Introduction:

      Tissue engineering and regenerative medicine hold great promise for addressing the challenges of tissue repair and regeneration. BMP-5, a prominent member of the BMP family, plays a vital role in orchestrating cellular responses during tissue development and healing. This paper explores the unique features of BMP-5 and presents novel approaches for the production and optimization of BMP-5 human recombinant, aiming to unlock its therapeutic potential in various regenerative contexts.

      Characteristics and Signaling Pathways:

      BMP-5 is a secreted growth factor that belongs to the transforming growth factor-beta (TGF-β) superfamily. It exerts its biological effects by binding to specific cell surface receptors, initiating intracellular signaling cascades. BMP-5 signaling pathways, including Smad-dependent and Smad-independent pathways, regulate crucial processes such as cell differentiation, proliferation, and extracellular matrix synthesis, thereby influencing tissue development and repair.

      Production of BMP-5 Human Recombinant:

      Efficient production methodologies are crucial for harnessing the therapeutic potential of BMP-5 human recombinant. Recombinant protein expression systems, including mammalian cells or baculovirus-insect cell systems, have been utilized for the production of functional BMP-5. Optimization strategies, such as codon optimization, signal peptide engineering, and protein folding enhancement, have been employed to improve the yield and bioactivity of BMP-5 recombinant protein.

      Potential Therapeutic Applications:

      BMP-5 human recombinant holds tremendous potential in the field of tissue engineering and regenerative medicine. It plays a crucial role in bone formation, cartilage regeneration, and wound healing, making it a promising candidate for the treatment of skeletal disorders, osteochondral defects, and tissue injuries. Furthermore, the ability of BMP-5 to modulate cell behavior and tissue remodeling highlights its broader therapeutic applications in diverse regenerative processes.

      Conclusion:

      BMP-5 human recombinant emerges as a key regulator in tissue engineering and regenerative medicine, with significant implications for tissue repair and regeneration. Optimizing production methodologies and further elucidating its signaling mechanisms will enhance its therapeutic applications. With its involvement in bone and cartilage formation, as well as wound healing, BMP-5 human recombinant represents a promising tool for promoting tissue regeneration and addressing the challenges of tissue repair in various clinical contexts.

      What is the molecular weight/Mw of BMP5 Protein?
      BMP5 Protein has a total Mw of 15.7kDa.

      What is the source or expression system of BMP5 Protein?
      Escherichia Coli.

      What is the Purity of BMP5 Protein?
      BMP5 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of BMP5 Protein?
      The biological functionality of BMP5 Protein will be determined in the future.

      What is the amino acid sequence of BMP5 Protein?
      MAANKRKNQN RNKSSSHQDS SRMSSVGDYN TSEQKQACKK HELYVSFRDL GWQDWIIAPE GYAAFYCDGE CSFPLNAHMN ATNHAIVQTL VHLMFPDHVP KPCCAPTKLN AISVLYFDDS SNVILKKYRN MVVRSCGCH.

      What applications can BMP5 Protein be used in?
      BMP5 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for BMP5 Protein?
      The endotoxin level is minimal, BMP5 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.

    Bmp 5 Human
  • View Data Sheet

    Name :

    SIRT6 Human

    Description:

    Sirtuin-6 Human Recombinant

    Mono-ADP-ribosyltransferase sirtuin-6, SIR2-like protein 6, SIRT6, SIR2L6, Sirtuin-6.

    Product # :

    PRO-282

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    Description

    SIRT6 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 375 amino acids (1-355 a.a.) and having a molecular mass of 41 kDa. Recombinant SIRT6 is fused to 20 amino acids His-tag at N-terminus and purified by conventional chromatography techniques.

    Source

    Escherichia Coli.

    Formulation

    The SIRT6 protein solution (1mg/ml) contains 20mM Tris-HCl pH-8 & 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      SIRT6 is part of the sirtuin family of proteins (Class IV), homologs to the yeast Sir2 protein. SIRT6 is characterized by a sirtuin core domain. Yeast sirtuin proteins are recognized by their ability to regulate epigenetic gene silencing and suppress recombination of rDNA. SIRT6, a chromatin-associated protein is involved in DNA repair. Human Sirtuins function as intracellular regulatory proteins with mono-ADP-ribosyltransferase activity.

    • Synonyms

      Mono-ADP-ribosyltransferase sirtuin-6, SIR2-like protein 6, SIRT6, SIR2L6, Sirtuin-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 MSVNYAAGLS PYADKGKCGL PEIFDPPEEL ERKVWELARL VWQSSSVVFH TGAGISTASG IPDFRGPHGV WTMEERGLAP KFDTTFESAR PTQTHMALVQ LERVGLLRFL VSQNVDGLHV RSGFPRDKLA ELHGNMFVEE CAKCKTQYVR DTVVGTMGLK ATGRLCTVAK ARGLRACRGE LRDTILDWED SLPDRDLALA DEASRNADLS ITLGTSLQIR PSGNLPLATK RRGGRLVIVN LQPTKHDRHA DLRIHGYVDE VMTRLMEHLG LEIPAWDGPR
      VLERALPPLP RPPTPKLEPK EESPTRINGS IPAGPKQEPC AQHNGSEPAS PKRERPTSPA PHRPPKRVKA KAVPS.

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    Sirt6 Human
  • View Data Sheet

    Name :

    C5 Human

    Description:

    Complement C5 Human

    Complement Component 5, C3 and PZP-Like Alpha-2-Macroglobulin Domain-Containing Protein 4, C5a Anaphylatoxin, Prepro-C5, CPAMD4, Anaphylatoxin C5a Analog, ECLZB, C5A, C5D, C5b, C5.

    Product # :

    PRO-2691

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    Description

    Human Complement C5 produced in Human plasma having a molecular mass of 190 kDa.

    Source

    Human Plasma.

    Formulation

    C5 protein solution contains PBS, pH 7.2.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Complement C5 is cleaved into C5a and C5b and is activated by all 3 pathways of complement activation. Each pathway of complement activation generates proteolytic enzyme complexes which binds to the target surface. These enzymes cleave a peptide bond in the larger alpha chain of C5 releasing the highly potent anaphylatoxin C5a and activating C5b. C5a has an imperative role in chemotaxis and C5b forms the 1st part of the complement membrane attack complex. Complement C5 is the 5th component of complement, which plays a central role in inflammatory and cell killing processes.

    • Synonyms

      Complement Component 5, C3 and PZP-Like Alpha-2-Macroglobulin Domain-Containing Protein 4, C5a Anaphylatoxin, Prepro-C5, CPAMD4, Anaphylatoxin C5a Analog, ECLZB, C5A, C5D, C5b, C5.

    • Physical Appearance

      Sterile filtered solution.

    • Stability

      C5 Human is stable at 4°C if entire vial will be used within 2-4 weeks.Store, frozen below -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.

    • Human Virus Test

      Plasma from each donor has been tested and found negative for antibody to HIV-1, HIV-2, HCV, HTLV-I &II, Syphillis and HBSAG.

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    C5 Human
  • View Data Sheet

    Name :

    CCDC25 Human

    Description:

    Coiled-Coil Domain Containing 25 Human Recombinant

    Coiled-coil domain-containing protein 25, CCDC25.

    Product # :

    PRO-1655

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    Description

    CCDC25 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 231 amino acids (1-208 a.a) and having a molecular mass of 26.9kDa.CCDC25 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    CCDC25 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Coiled-Coil Domain Containing 25 (CCDC25) is a 208 amino acid protein belonging to the CCDC25 family.

    • Synonyms

      Coiled-coil domain-containing protein 25, CCDC25.

    • 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 MGSMVFYFTS SSVNSSAYTI YMGKDKYENE DLIKHGWPED IWFHVDKLSS AHVYLRLHKG ENIEDIPKEV LMDCAHLVKA NSIQGCKMNN VNVVYTPWSN LKKTADMDVG QIGFHRQKDV KIVTVEKKVN EILNRLEKTK VERFPDLAAE KECRDREERN EKKAQIQEMK KREKEEMKKK REMDELRSYS SLMKVENMSS NQDGNDSDEF M.

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    Ccdc25 Human
  • View Data Sheet

    Name :

    SNCG Human

    Description:

    Gamma-Synuclein Human Recombinant

    Gamma-synuclein, Persyn, Breast cancer-specific gene 1 protein, Synoretin, SR, SNCG, BCSG1, PERSYN, PRSN, g-Synuclein.

    Product # :

    PRO-395

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    Description

    g-Synuclein Human Recombinant produced in E.Coli is a single,non-glycosylated polypeptide chain containing 127 amino acids and having a molecular mass of 13,300 Dalton. The protein coding region of g-synuclein was amplified by RT-PCR and cloned into an E.coli expression vector. g-synuclein was overexpressed in E. coli and purified to apparent homogeneity by taking advantage of the thermosolubility of the protein and by using conventional column chromatography techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein (1mg/ml) contains 20mM Tris-HCl buffer (pH 7.5) and 0.1M NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      g-synuclein(Originally known as a breast cancer specific gene product, BCSG1) is an acidic neuronal protein of 127 amino acids. Gamma-Synuclein is a member of the Synuclein protein family, which is believed to be involved in the pathogenesis of neurodegenerative diseases. High levels of Gamma-Synuclein have been found in advanced breast carcinomas suggesting a correlation between overexpression of SNCG and breast tumor development. Synuclein-Gamma is found mostly in the peripheral nervous system (in primary sensory neurons, sympathetic neurons, and motor neurons) and retina. SNCG is also identified in the brain, ovarian tumors, and in the olfactory epithelium. SNCG expression in breast tumors is a marker for tumor progression. A modification in the expression of gamma-synuclein has been detected in the retina of Alzheimer's patients.

    • Synonyms

      Gamma-synuclein, Persyn, Breast cancer-specific gene 1 protein, Synoretin, SR, SNCG, BCSG1, PERSYN, PRSN, g-Synuclein.

    • 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

      MDVFKKGFSI AKEGVVGAVE KTKQGVTEAA EKTKEGVMYV GAKTKENVVQSVTSVAEKTK EQANAVSEAV VSSVNTVATK TVEEAENIAV TSGVVRKEDL RPSAPQQEGV ASKEKEEVAE EAQSGGD.

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    Sncg Human
  • View Data Sheet

    Name :

    ASB13 Human

    Description:

    Ankyrin Repeat And SOCS Box Containing 13 Human Recombinant

    Ankyrin repeat and SOCS box protein 13, ASB-13, ASB13, ankyrin repeat and SOCS box containing 13.

    Product # :

    PRO-2060

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    Description

    ASB13 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 301 amino acids (1-278 a.a.) and having a molecular mass of 32.4kDa.ASB13 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ASB13 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 0.4M UREA and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      ASB13 belongs to the ankyrin repeat and SOCS box-containing (ASB) family of proteins which contains ankyrin repeat sequence and a SOCS box domain. ASB13 is a protein coding gene that plays a role as a substrate-recognition part of a SCF-like ECS E3 ubiquitin-protein ligase complex which arbitrates the ubiquitination and subsequent proteasomal degradation of target proteins.

    • Synonyms

      Ankyrin repeat and SOCS box protein 13, ASB-13, ASB13, ankyrin repeat and SOCS box containing 13.

    • 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).Please avoid freeze thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMEPRAAD GCFLGDVGFW VERTPVHEAA QRGESLQLQQ LIESGACVNQ VTVDSITPLH AASLQGQARC VQLLLAAGAQ VDARNIDGST PLCDACASGS IECVKLLLSY GAKVNPPLYT ASPLHEACMS GSSECVRLLI DVGANLEAHD CHFGTPLHVA CAREHLDCVK VLLNAGANVN AAKLHETALH HAAKVKNVDL IEMLIEFGGN IYARDNRGKK PSDYTWSSSA PAKCFEYYEK TPLTLSQLCR VNLRKATGVR GLEKIAKLNI PPRLIDYLSY N.

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    Asb13 Human
  • View Data Sheet

    Name :

    Protein-L Cys, His

    Description:

    Protein-L Cys Recombinant, His Tag

    Product # :

    PRO-1932

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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 and a Cys on C-terminus. Protein-L is comprised of 5 IgG-binding regions of protein L (B1-B2-B3-B4-B5) containing 373 amino acids in total and having a molecular mass of 41.6kDa, 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 96.0% as determined 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 AGC.

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    Protein L Cys His
  • View Data Sheet

    Name :

    ARFIP1 Human

    Description:

    ADP-Ribosylation Factor Interacting Protein 1 Human Recombinant

    HSU52521, Arfaptin-1, ADP-ribosylation factor-interacting protein 1.

    Product # :

    PRO-2088

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    Description

    ARFIP1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 396 amino acids (1-373 a.a) and having a molecular mass of 44.1kDa.ARFIP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ARFIP1 protein solution (0.25mg/ml) containing Phosphate buffered saline (pH7.4), 20% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      ADP-Ribosylation Factor Interacting Protein 1 (ARFIP1) contains 1 AH domain and is a putative target protein of ADP-ribosylation factor.

    • Synonyms

      HSU52521, Arfaptin-1, ADP-ribosylation factor-interacting protein 1.

    • 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 MGSMAQESPK NSAAEIPVTS NGEVDDSREH SFNRDLKHSL PSGLGLSETQ ITSHGFDNTK EGVIEAGAFQ GSPAPPLPSV MSPSRVAASR LAQQGSDLIV PAGGQRTQTK SGPVILADEI KNPAMEKLEL VRKWSLNTYK CTRQIISEKL GRGSRTVDLE LEAQIDILRD NKKKYENILK LAQTLSTQLF QMVHTQRQLG DAFADLSLKS LELHEEFGYN ADTQKLLAKN GETLLGAINF FIASVNTLVN KTIEDTLMTV KQYESARIEY DAYRTDLEEL NLGPRDANTL PKIEQSQHLF QAHKEKYDKM RNDVSVKLKF LEENKVKVLH NQLVLFHNAI AAYFAGNQKQ LEQTLKQFHI KLKTPGVDAP SWLEEQ.

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    Arfip1 Human
  • View Data Sheet

    Name :

    GCSAM Human

    Description:

    Germinal Center-Associated, Signaling and Motility Human Recombinant

    GCAT2, HGAL, Germinal center-associated signaling and motility protein, Germinal center B-cell-expressed transcript 2 protein, Germinal center-associated lymphoma protein, GAL, GCET2 .

    Product # :

    PRO-1282

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    • More Info

    Description

    GCSAM Human Recombinant produced in E. coli is a single polypeptide chain containing 201 amino acids (1-178) and having a molecular mass of 23 kDa. GCSAM is fused to 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The GCSAM solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol and 1mM DTT.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      GCSAM is a protein which functions in signal transduction pathways and whose expression raises in germinal cell lymphomas. GCSAM contains a putative PDZ-interacting domain, an immunoreceptor tyrosine-based activation motif (ITAM), and two putative SH2 binding sites. In B cells, GCSAM expression is particularly induced by interleukin-4.

    • Synonyms

      GCAT2, HGAL, Germinal center-associated signaling and motility protein, Germinal center B-cell-expressed transcript 2 protein, Germinal center-associated lymphoma protein, GAL, GCET2 .

    • 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 MGSMGNSLLR ENRRQQNTQE MPWNVRMQSP KQRTSRCWDH HIAEGCFCLP WKKILIFEKR QDSQNENERM SSTPIQDNVD QTYSEELCYT LINHRVLCTR PSGNSAEEYY ENVPCKAERP RESLGGTETE YSLLHMPSTD PRHARSPEDE YELLMPHRIS SHFLQQPRPL MAPSETQFSH L.

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

    Gcsam Human
  • View Data Sheet

    Name :

    KCNMB3 Human

    Description:

    KCNMB3 Human Recombinant

    Potassium Channel Subfamily M Regulatory Beta Subunit 3, Potassium Large Conductance Calcium-Activated Channel, Subfamily M Beta Member 3, Calcium-Activated Potassium Channel, Subfamily M Subunit Beta-3, Charybdotoxin Receptor Subunit Beta-3, Big Potassium Channel Beta Subunit 3, Maxi K Channel Subunit Beta-3, MaxiK Channel Beta-Subunit 3, BK Channel Beta Subunit 3, BK Channel Subunit Beta-3, K(VCA)BETA-3, SLO-BETA-3, BKBETA3, Hbeta3, KCNMB2, KCNMBL, Large Conductance, Voltage And Ca2+ Activated Potassium Channel Maxi K Beta 3 Subunit, Calcium-Activated Potassium Channel Regulatory Subunit, SLOBETA3, Calcium-activated potassium channel subunit beta-3.

    Product # :

    PRO-2072

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    KCNMB3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 149 amino acids (82-207 a.a) and having a molecular mass of 16.8kDa. KCNMB3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    KCNMB3 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      The KCNMB3 belongs to a family of 4 auxiliary beta subunits found in the mammalian genome, which associate with Slo1 alpha subunits and regulate BK channel function. In humans, the KCNMB3 gene is comprised of 4 N-terminal alternative exons which produce 4 functionally distinct beta3 subunits, beta3a-d. Three variants, beta3a-c, display kinetically distinct inactivation behaviors.

    • Synonyms

      Potassium Channel Subfamily M Regulatory Beta Subunit 3, Potassium Large Conductance Calcium-Activated Channel, Subfamily M Beta Member 3, Calcium-Activated Potassium Channel, Subfamily M Subunit Beta-3, Charybdotoxin Receptor Subunit Beta-3, Big Potassium Channel Beta Subunit 3, Maxi K Channel Subunit Beta-3, MaxiK Channel Beta-Subunit 3, BK Channel Beta Subunit 3, BK Channel Subunit Beta-3, K(VCA)BETA-3, SLO-BETA-3, BKBETA3, Hbeta3, KCNMB2, KCNMBL, Large Conductance, Voltage And Ca2+ Activated Potassium Channel Maxi K Beta 3 Subunit, Calcium-Activated Potassium Channel Regulatory Subunit, SLOBETA3, Calcium-activated potassium channel subunit beta-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 MGSKPFMLSI QREESTCTAI HTDIMDDWLD CAFTCGVHCH GQGKYPCLQV FVNLSHPGQK ALLHYNEEAV QINPKCFYTP KCHQDRNDLL NSALDIKEFF DHKNGTPFSC FYSPASQSED VILIKKYDQ.

    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.

    Kcnmb3 Human
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