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  • View Data Sheet

    Description:

    Platelet-Derived Growth Factor BB Mouse Recombinant

    Glioma-derived growth factor, GDGF, Osteosarcoma-derived Growth Factor, ODGF, SIS, SSV, PDGF2, c-sis, FLJ12858, PDGF-BB, PDGF B-chain, Platelet-derived growth factor beta polypeptide, Becaplermin.

    Product # :

    CYT-412

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    Description

    Platelet-Derived Growth Factor BB Mouse Recombinant produced in E.coli, is a homodimeric, non-glycosylated, polypeptide chain containing 2x110 (total of 2 chains 220aa) amino acids and having a total molecular weight of 24.7 kDa.PDGF-BB is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from 10mM NaCitrate pH-3.0.

    Purity

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

    Biological Activity

    The biological activity is determined by the dose-dependant stimulation of the proliferation of human umbelical vein endothelial cells (HUVEC) using a concentration range of less than 1.6ng/ml.

    More Info

    • Introduction

      PDGF-BB is a member of the platelet-derived growth factor family. The four members of this family are mitogenic factors for cells of mesenchymal origin and are characterized by a motif of eight cysteines. This gene product can exist either as a homodimer (PDGF-BB) or as a heterodimer with the platelet-derived growth factor alpha polypeptide (PDGF-AB), where the dimers are connected by disulfide bonds. Mutations in this gene are associated with meningioma. Reciprocal translocations between chromosomes 22 and 7, at sites where this gene and that for COL1A1 are located, are associated with a particular type of skin tumor called dermatofibrosarcoma protuberans resulting from unregulated expression of growth factor. Two splice variants have been identified for this gene.

    • Synonyms

      Glioma-derived growth factor, GDGF, Osteosarcoma-derived Growth Factor, ODGF, SIS, SSV, PDGF2, c-sis, FLJ12858, PDGF-BB, PDGF B-chain, Platelet-derived growth factor beta polypeptide, Becaplermin.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Platelet-derived Growth Factor BB although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution PDGF BB 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 Platelet-derived Growth Factor-BB in sterile 100mM acetic acid and 0.1% BSA not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MSLGSLAAAE PAVIAECKTR TEVFQISRNL IDRTNANFLV WPPCVEVQRC SGCCNNRNVQ CRASQVQMRP VQVRKIEIVR KKPIFKKATV TLEDHLACKC ETIVTPRPVT

    • Background

      Platelet-Derived Growth Factor BB (PDGF-BB) is one of the isoforms of the PDGF family that plays a significant role in embryonic development, cell proliferation, cell migration, and angiogenesis.

      It's also relevant in the context of certain pathologies like cancer or healing processes.

      Here's what a research paper on Mouse Recombinant PDGF-BB might involve:

      Basic Biology:

      It might discuss the basic biology and function of PDGF-BB in the mouse model. This could include its role in various cellular processes like cell growth, division, and survival, as well as in the context of tissue repair or angiogenesis.

      Recombinant PDGF-BB Production:

      The paper might describe methods for producing recombinant PDGF-BB in laboratory conditions. It might go into detail on the expression system used (e.g., bacterial, yeast, or mammalian cells), the purification process, and how the functionality of the produced PDGF-BB was confirmed.

      Applications:

      It could also detail the experimental applications of recombinant PDGF-BB in the mouse model. For instance, it could be used to study wound healing processes, tissue regeneration, or the development and progression of certain diseases.

      Comparative Analysis:

      The research might include a comparison of the recombinant PDGF-BB with its natural counterpart in terms of functionality, structure, or other properties.

      Innovation:

      If the paper is presenting new research, it might discuss an innovative use of PDGF-BB, a novel production method, or new findings about its function.

    • Protein content

      Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.48 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of PDGF-BB as a Reference Standard.

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

    Pdgf Bb Mouse
  • View Data Sheet

    Description:

    Coiled-Coil-Helix-Coiled-Coil-Helix Domain Containing 3 Human Recombinant

    Regulatory Subunit 22, MINOS3, PPP1R22, Mitochondrial Inner Membrane Organizing System 3, Protein Phosphatase 1, Coiled-Coil-Helix-Coiled-Coil-Helix Domain-Containing Protein 3 Mitochondrial, Protein Phosphatase 1, Regulatory Subunit 22.

    Product # :

    PRO-815

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    Description

    CHCHD3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 250 amino acids (1-227 a.a) and having a molecular mass of 28.5kDa.CHCHD3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CHCHD3 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol and 2mM DTT.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Coiled-coil-helix-coiled-coil-helix domain containing 3 (CHCHD3), is a protein-coding gene. CHCHD3 is essential for maintenance of mitochondrial crista integrity and mitochondrial function. . In addition, CHCHD3 may perform as a scaffolding protein that stabilizes protein complexes involved in crista architecture and protein import. CHCHD3 may also act as a transcription factor which binds to the BAG1 promoter and represses BAG1 transcription. Lung cancer has been associated with CHCHD3.

    • Synonyms

      Regulatory Subunit 22, MINOS3, PPP1R22, Mitochondrial Inner Membrane Organizing System 3, Protein Phosphatase 1, Coiled-Coil-Helix-Coiled-Coil-Helix Domain-Containing Protein 3 Mitochondrial, Protein Phosphatase 1, Regulatory Subunit 22.

    • 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 MGSMGGTTST RRVTFEADEN ENITVVKGIR LSENVIDRMK ESSPSGSKSQ RYSGAYGASV SDEELKRRVA EELALEQAKK ESEDQKRLKQ AKELDRERAA ANEQLTRAIL RERICSEEER AKAKHLARQL EEKDRVLKKQ DAFYKEQLAR LEERSSEFYR VTTEQYQKAA EEVEAKFKRY ESHPVCADLQ AKILQCYREN THQTLKCSAL ATQYMHCVNH AKQSMLEKGG

    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.

    Chchd3 Human
  • View Data Sheet

    Description:

    Activated Leukocyte Cell Adhesion Molecule (CD166) Mouse Recombinant

    Activated leukocyte cell adhesion molecule, ALCAM, Alcam, CD166 antigen, CD166 antigen isoform1, CD166, Protein DM-GRASP, AI853494 Protein, MuSC, SC1, BEN.

    Product # :

    PRO-2749

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    Description

    ALCAM mouse produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 739 amino acids (28-527a.a.) and having a molecular mass of 83.1kDa. ALCAM is expressed with a 239 amino acid hIgG-His-Tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    ALCAM protein solution (0.25mg/ml) contains 50% glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Measured by its ability to block the adhesion of Jurkat human acute T cell leukemia cells to immobilized Recombinant Human CD6. When cells are added to 1 ug/ml of mouse ALCAM binded to CD6, this effect is more to 50%.

    More Info

    • Introduction

      CD166 antigen isoform 2 (ALCAM) is a type 1 membrane glycoprotein and belongs to the immunoglobulin superfamily. ALCAM is expressed on thymic epithelium, microvascular endothelium, activated lymphocytes and monocytes, and monocyte-derived dendritic cells. CD166 and CD6 interaction plays a role in T cell development and T cell regulation, as well as in the binding of T cells and B cells to activated leukocytes.

    • Synonyms

      Activated leukocyte cell adhesion molecule, ALCAM, Alcam, CD166 antigen, CD166 antigen isoform1, CD166, Protein DM-GRASP, AI853494 Protein, MuSC, SC1, BEN.

    • 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

      WYTVNSAYGD TIVMPCRLDV PQNLMFGKWK YEKPDGSPVF IAFRSSTKKS VQYDDVPEYK DRLSLSENYT LSIANAKISD EKRFVCMLVT EDNVFEAPTL VKVFKQPSKP EIVNKAPFLE TDQLKKLGDC ISRDSYPDGN ITWYRNGKVL QPVEGEVAIL FKKEIDPGTQ LYTVTSSLEY KTTRSDIQMP FTCSVTYYGP SGQKTIYSEQ EIFDIYYPTE QVTIQVLPPK NAIKEGDNIT
      LQCLGNGNPP PEEFMFYLPG QPEGIRSSNT YTLTDVRRNA TGDYKCSLID KRNMAASTTI TVHYLDLSLN PSGEVTKQIG DTLPVSCTIS ASRNATVVWM KDNIRLRSSP SFSSLHYQDA GNYVCETALQ EVEGLKKRES LTLIVEGKPQ IKMTKKTDPS GLSKTIICHV EGFPKPAIHW TITGSGSVIN QTEESPYING RYYSKIIISP EENVTLTCTA ENQLERTVNS LNVSAISIPE
      HDEADDISDE NREKVNDQAK LEPKSCDKTH TCPPCPAPEL LGGPSVFLFP PKPKDTLMIS RTPEVTCVVV DVSHEDPEVK FNWYVDGVEV HNAKTKPREE QYNSTYRVVS VLTVLHQDWL NGKEYKCKVS NKALPAPIEK TISKAKGQPR EPQVYTLPPS RDELTKNQVS LTCLVKGFYP SDIAVEWESN GQPENNYKTT PPVLDSDGSF FLYSKLTVDK SRWQQGNVFS CSVMHEALHN HYTQKSLSLS PGK HHHHHH

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

    Cd166 Mouse
  • View Data Sheet

    Description:

    Interleukin-7 Human Recombinant, Yeast

    Lymphopoietin 1 (LP-1), pre-B cell factor, IL-7.

    Product # :

    CYT-298

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    Description

    Interleukin-7 Human Recombinant produced in yeast is a single, glycosylated polypeptide chain containing 152 amino acids and having a molecular mass of 17.4 kDa. The IL-7 is purified by proprietary chromatographic techniques.

    Source

    Saccharomyces cerevisiae.

    Formulation

    Lyophilized from a concentrated (1mg/ml) solution in water containing 20mM phosphate buffer.

    Purity

    Greater than 98.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 as determined by the dose-dependent stimulation of thymidine uptake by murine pre-B cell line 2E8 is < 0.5 ng/ml, corresponding to a specific activity of > 2 x 106 units/mg.

    More Info

    • Introduction

      IL-7 is a cytokine important for B and T cell development. This cytokine and the hepatocyte growth factor (HGF) form a heterodimer that functions as a pre-pro-B cell growth-stimulating factor. This cytokine is found to be a cofactor for V(D)J rearrangement of the T cell receptor beta (TCRB) during early T cell development. This cytokine can be produced locally by intestinal epithelial and epithelial goblet cells, and may serve as a regulatory factor for intestinal mucosal lymphocytes. Knockout studies in mice suggested that this cytokine plays an essential role in lymphoid cell survival.

    • Synonyms

      Lymphopoietin 1 (LP-1), pre-B cell factor, IL-7.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Interleukin-7 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL7 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Interleukin -7 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      The sequence of the first five N-terminal amino acids was determined and was found to be Asp-Cys-Asp-Ile-Glu.

    • Background

      What is the molecular weight/Mw of IL7 HUMAN, YEAST Protein?
      IL7 HUMAN, YEAST Protein has a total Mw of 17.4kDa.

      What is the source or expression system of IL7 HUMAN, YEAST Protein?
      Saccharomyces cerevisiae.

      What is the Purity of IL7 HUMAN, YEAST Protein?
      IL7 HUMAN, YEAST Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL7 HUMAN, YEAST Protein?
      The ED50 as determined by the dose-dependent stimulation of thymidine uptake by murine pre-B cell line 2E8 is < 0.5 ng/ml, corresponding to a specific activity of > 2 x 106 units/mg.

      What is the amino acid sequence of IL7 HUMAN, YEAST Protein?
      The sequence of the first five N-terminal amino acids was determined and was found to be Asp-Cys-Asp-Ile-Glu.

      What applications can IL7 HUMAN, YEAST Protein be used in?
      IL7 HUMAN, YEAST Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IL7 HUMAN, YEAST Protein?
      The endotoxin level is minimal, IL7 HUMAN, YEAST Protein was purified using conventional chromatography techniques.

      Who supplies recombinant IL7 HUMAN, YEAST that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of IL7 HUMAN, YEAST?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

    • Protein content

      Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.418 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of IL-7 as a Reference Standard.

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

    Il 7 Human Yeast
  • View Data Sheet

    Description:

    Triggering Receptor Expressed on Myeloid Cells 2 Human Recombinant, HEK

    Triggering receptor expressed on myeloid cells 2, Triggering receptor expressed on monocytes 2, TREM-2, TREM2, Trem2a, Trem2b, Trem2c.

    Product # :

    PRO-2773

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    Description

    TREM2 Human Recombinant is a single, glycosylated, polypeptide chain (19-174 a.a) containing a total of 162 amino acids, having a molecular mass of 18.2 kDa. TREM2 is fused to a 6 amino acid His-tag at C-terminus and is purified by proprietary chromatographic techniques.

    Source

    HEK293 Cells.

    Formulation

    The TREM2 solution (1mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Synonyms

      Triggering receptor expressed on myeloid cells 2, Triggering receptor expressed on monocytes 2, TREM-2, TREM2, Trem2a, Trem2b, Trem2c.

    • 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

      HNTTVFQGVA GQSLQVSCPY DSMKHWGRRK AWCRQLGEKG PCQRVVSTHN LWLLSFLRRW NGSTAITDDT LGGTLTITLR NLQPHDAGLY QCQSLHGSEA DTLRKVLVEV LADPLDHRDA GDLWFPGESE SFEDAHVEHS ISRSLLEGEI PFPPTSHHHH HH.

    • Background

      TREM2 (Triggering Receptor Expressed on Myeloid Cells 2) is a transmembrane glycoprotein predominantly expressed on microglia, macrophages, and dendritic cells. In recent years, TREM2 has emerged as a key regulator of immune responses in the central nervous system (CNS). This research paper aims to provide an in-depth analysis of the function, signaling pathways, and pathological implications of TREM2 human recombinant. Additionally, it explores the potential therapeutic applications of targeting TREM2 in various neurological disorders. This study will contribute to a better understanding of the role of TREM2 in immune modulation and its potential as a therapeutic target.

      The Functions of TREM-2: TREM-2 functions as a critical regulator of microglial and macrophage responses in the central nervous system. It is involved in various cellular processes, including phagocytosis, cytokine production, immune cell activation, and cell survival. Additionally, TREM-2 influences microglial polarization, leading to distinct phenotypes with either pro-inflammatory or anti-inflammatory properties. Understanding the multifaceted functions of TREM-2 is essential for unraveling its contributions to immune homeostasis and disease pathogenesis.

      Signaling Pathways and Mechanisms: TREM-2 exerts its effects through complex signaling pathways. Upon activation, TREM-2 interacts with adaptor proteins and triggers downstream signaling cascades involving kinases, phosphatases, and transcription factors. These signaling events modulate immune responses, including the production of cytokines, chemokines, and growth factors. Elucidating the intricate mechanisms underlying TREM-2 signaling is vital for comprehending its role in immune regulation and exploring potential therapeutic interventions.

      Implications in Neurodegenerative Diseases: TREM-2 has emerged as a key player in neurodegenerative diseases, such as Alzheimer's disease, Parkinson's disease, and frontotemporal dementia. Dysregulation of TREM-2 expression and function is associated with altered immune responses, impaired phagocytosis, and neuroinflammation, which contribute to disease progression. Investigating the involvement of TREM-2 in neurodegenerative disorders enhances our understanding of the underlying pathological mechanisms and offers potential therapeutic avenues for intervention.

      Conclusion: The TREM-2 protein plays a critical role in immune modulation and neuroinflammation in the central nervous system. This comprehensive investigation sheds light on the multifaceted functions, signaling pathways, and implications of TREM-2, particularly in the context of neurodegenerative diseases. Further exploration of TREM-2's role may pave the way for novel therapeutic strategies targeting this protein, with the potential to mitigate immune dysregulation and neuroinflammatory processes in various neurological conditions.

      Note: Due to the nature of this response, a bibliography could not be provided. However, I encourage you to consult scientific literature and research articles on TREM-2 for a comprehensive list of references and sources.

    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.

    Trem2 Human Hek
  • View Data Sheet

    Description:

    Macrophage-Colony Stimulating Factor Rat Recombinant

    Macrophage colony-stimulating factor 1, CSF-1, MCSF, Csf1, Csfm.

    Product # :

    CYT-856

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    Description

    Macrophage Colony Stimulating Factor Rat Recombinant produced in E.coli is a non-glycosylated homodimer, containing 2 x 155 amino acids and having a total molecular mass of 36.2 kDa.MCSF is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a sterile filtered aqueous solution containing 10mM Na3PO4, pH 7.5.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The activity as determined by dose-dependent induction of M-NFS-60 cell proliferation is 1.65 ng/ml. This corresponds to an expected specific activity of 6.1x105 units/mg.

    More Info

    • Introduction

      Granulocyte/Macrophage Colony-Stimulating Factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. MCSF induces cells of the monocyte/macrophage lineage. MCSF plays a role in immunological defenses, bone metabolism, lipoproteins clearance, fertility and pregnancy.

    • Synonyms

      Macrophage colony-stimulating factor 1, CSF-1, MCSF, Csf1, Csfm.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MEVSEHCSHM IGNGHLQILQ QLIDSQMETA CLIEYKFVDQ EQLDDPVCYL KKAFVLVQVI IEETMRFKDN TPNANATERL QELSMKLNSC FIKDYKEQNE ACVQTYKESP LRLLEKIKNF FNETKNFLEK DWNIFSKNCN DSLAKCSSRD VVTKP.

    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.

    Mcsf Rat
  • View Data Sheet

    Description:

    PDZ Domain Containing 11 Human Recombinant

    PDZ domain-containing protein 11, ATPase-interacting PDZ protein, Plasma membrane calcium ATPase-interacting single-PDZ protein, PMCA-interacting single-PDZ protein, PDZD11, AIPP1, PDZK11, PISP.

    Product # :

    PRO-1263

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    Description

    PDZD11 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 163 amino acids (1-140 a.a) and having a molecular mass of 18.5kDa.PDZD11 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PDZD11 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      PDZ Domain Containing 11 (PDZD11) is a cytosolic protein which contains one PDZ (DHR) domain. PDZD11 displays a resemblance to members of the MALS / VELIS family of proteins. PDZD11 contains but one PDZ domain which seemingly interacts with the C-terminus of partner proteins. PDZD11 is ubiquitously expressed and targets calcium and copper ATPases to basolateral cell membranes. PDZD11 is a briefly interacting partner of the PMCA b-splice forms which have a role in their sorting to or from the plasma membrane.

    • Synonyms

      PDZ domain-containing protein 11, ATPase-interacting PDZ protein, Plasma membrane calcium ATPase-interacting single-PDZ protein, PMCA-interacting single-PDZ protein, PDZD11, AIPP1, PDZK11, PISP.

    • 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 MGSMDSRIPY DDYPVVFLPA YENPPAWIPP HERVHHPDYN NELTQFLPRT ITLKKPPGAQ LGFNIRGGKA SQLGIFISKV IPDSDAHRAG LQEGDQVLAV NDVDFQDIEH SKAVEILKTA REISMRVRFF PYNYHRQKER TVH.

    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.

    Pdzd11 Human
  • View Data Sheet

    Description:

    Ubiquitin Conjugating Enzyme E2D2 Human Recombinant, His Tag

    ubiquitin-conjugating enzyme E2D 2 (homologous to yeast UBC4/5), UBC4, Ubiquitin carrier protein D2, Ubiquitin-conjugating enzyme E2-17 kDa 2, Ubiquitin-protein ligase D2, UBCH5B, EC 6.3.2.19, E2(17)KB2, PUBC1, UBC4/5, UBC5B, UBCH4.

    Product # :

    ENZ-154

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    Description

    UBE2D2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 167 amino acids (1-147) and having a molecular mass of 18.9 kDa.The UBE2D2 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The UBE2D2 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 0.1M NaCl and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      UBE2D2 belongs to the E2 ubiquitin-conjugating enzyme family. UBE2D2 takes part in the ubiquitination of the tumor-suppressor protein p53, which is induced by an E3 ubiquitin-protein ligase. UBE2D2 catalyzes ubiquitination of IkB-alpha in a SCFB-TRCP and phosphorylation dependent method.

    • Synonyms

      ubiquitin-conjugating enzyme E2D 2 (homologous to yeast UBC4/5), UBC4, Ubiquitin carrier protein D2, Ubiquitin-conjugating enzyme E2-17 kDa 2, Ubiquitin-protein ligase D2, UBCH5B, EC 6.3.2.19, E2(17)KB2, PUBC1, UBC4/5, UBC5B, UBCH4.

    • 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 MALKRIHKEL NDLARDPPAQ CSAGPVGDDM FHWQATIMGP NDSPYQGGVF FLTIHFPTDY PFKPPKVAFT TRIYHPNINS NGSICLDILR SQWSPALTIS KVLLSICSLL CDPNPDDPLV PEIARIYKTD REKYNRIARE WTQKYAM.

    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.

    Ube2D2 Human
  • View Data Sheet

    Description:

    Geranylgeranyl Diphosphate Synthase 1 Human Recombinant

    GGPPS, GGPPS1, GGPP synthetase.

    Product # :

    ENZ-555

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    Description

    GGPS1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 320 amino acids (1-300 a.a.) and having a molecular mass of 37 kDa. The GGPS1 is fused to a 20 amino acids His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GGPS1 Human recombinant (1mg/ml) protein solution contains 20mM Tris-HCl pH-8, 1mM DTT & 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      GGPS1 is PART of the prenyltransferase family. GGPS1 is widely expressed in testis, heart and skeletal muscle, GGPS1 is localized in the cytoplasm and catalyzes the formation of geranylgeranyl pyrophosphate, a precursor of geranylgeranylated proteins and carotenoids. GGPS1 is a significant enzyme that is responsible for the C20-prenylation of proteins and for the regulation of a nuclear hormone receptor.

    • Synonyms

      GGPPS, GGPPS1, GGPP synthetase.

    • 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 MEKTQETVQR ILLEPYKYLL QLPGKQVRTK LSQAFNHWLK VPEDKLQIII EVTEMLHNAS LLIDDIEDNS KLRRGFPVAH SIYGIPSVIN SANYVYFLGL EKVLTLDHPD AVKLFTRQLL ELHQGQGLDI YWRDNYTCPT EEEYKAMVLQ KTGGLFGLAV
      GLMQLFSDYK EDLKPLLNTL GLFFQIRDDY ANLHSKEYSE NKSFCEDLTE GKFSFPTIHA IWSRPESTQV QNILRQRTEN IDIKKYCVHY LEDVGSFEYT RNTLKELEAK AYKQIDARGG NPELVALVKH LSKMFKEENE.

    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.

    Ggps1 Human
  • View Data Sheet

    Description:

    CD14 Clone PAT87H7AT, Mouse Anti Human

    Monocyte differentiation antigen CD14, Myeloid cell-specific leucine-rich glycoprotein.

    Product # :

    ANT-565

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    Formulation

    1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.

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    • Introduction

      CD14 (also known lipopolysaccharide (LPS) receptor) is expressed strongly on monocytes and macrophage and weakly on the surface of neutrophils. CD14 is anchored to cells by linkage to glycosylphosphatidylinositol (GPI) and functions as a high affinity receptor for complexes of LPS and LPS binding protein (LBP). Soluble CD14, also binding to LPS, acts at physiological concentration as an LPS agonist and has, at higher concentrations, an LPS antagonizing effect in cell activation. CD14 has been shown to bind apoptotic cells.

    • Synonyms

      Monocyte differentiation antigen CD14, Myeloid cell-specific leucine-rich glycoprotein.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Anti-human CD14 mAb, clone PAT87H7AT, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human CD14 protein 20-349 amino acids purified from E. coli.

    • Ig Subclass

      Mouse IgG2b heavy chain and k light chain.

    • Clone

      PAT87H7AT.

    • Applications

      The antibody has been tested by ELISA, Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

      For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.

    • Purification Method

      CD14 antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.

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

    Cd14 Pat87H7At Antibody
  • View Data Sheet

    Description:

    Mitogen-Activated Protein Kinase Kinase 3 Human Recombinant

    Dual specificity mitogen-activated protein kinase kinase 3, MAP kinase kinase 3, MAPKK 3, MAPK/ERK kinase 3, MEK 3, MAP2K3, MEK3, MKK3, PRKMK3.

    Product # :

    PKA-004

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    Description

    MAP2K3 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 338 amino acids (1-318) and having a molecular mass of 38.3kDa. MAP2K3 is fused to 20 a.a. His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MAP2K3 solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Dual specificity mitogen-activated protein kinase kinase 3 (MAP2K3) is a dual specificity protein kinase which is a member of the MAP kinase kinase family. MAP2K3 is activated by mitogenic and environmental stress, and participates in the MAP kinase-mediated signaling cascade. MAP2K3 phosphorylates and consequently activates MAPK14/p38-MAPK.

    • Synonyms

      Dual specificity mitogen-activated protein kinase kinase 3, MAP kinase kinase 3, MAPKK 3, MAPK/ERK kinase 3, MEK 3, MAP2K3, MEK3, MKK3, PRKMK3.

    • 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 MSKPPAPNPT PPRNLDSRTF ITIGDRNFEV EADDLVTISE LGRGAYGVVE KVRHAQSGTI MAVKRIRATV NSQEQKRLLM DLDINMRTVD CFYTVTFYGA LFREGDVWIC MELMDTSLDK FYRKVLDKNM TIPEDILGEI AVSIVRALEH LHSKLSVIHR DVKPSNVLIN KEGHVKMCDF GISGYLVDSV AKTMDAGCKP YMAPERINPE LNQKGYNVKS DVWSLGITMI EMAILRFPYE SWGTPFQQLK QVVEEPSPQL PADRFSPEFV DFTAQCLRKN PAERMSYLEL MEHPFFTLHK TKKTDIAAFV KEILGEDS.

    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.

    Map2K3 Human
  • View Data Sheet

    Description:

    5'-Nucleotidase Ecto (CD73) Human Recombinant

    NT, eN, NT5, NTE, eNT, CD73, E5NT, 5'-nucleotidase, 5'-NT, Ecto-5'-nucleotidase, NT5E.

    Product # :

    PRO-1853

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    Description

    NT5E (CD73) Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 247amino acids (27-252 a.a) and having a molecular mass of 27kDa. NT5E (CD73) is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    NT5E (CD73) protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

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    • Introduction

      NT5E, also known as CD73, is a plasma membrane protein which catalyzes the conversion of extracellular nucleotides into membrane-permeable nucleosides. NT5E is functions as a determinant of lymphocyte differentiation. Defects in NT5E can cause the calcification of joints and arteries.

    • Synonyms

      NT, eN, NT5, NTE, eNT, CD73, E5NT, 5'-nucleotidase, 5'-NT, Ecto-5'-nucleotidase, NT5E.

    • 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 MWELTILHTN DVHSRLEQTS EDSSKCVNAS RCMGGVARLF TKVQQIRRAE PNVLLLDAGD QYQGTIWFTV YKGAEVAHFM NALRYDAMAL GNHEFDNGVE GLIEPLLKEA KFPILSANIK AKGPLASQIS GLYLPYKVLP VGDEVVGIVG YTSKETPFLS NPGTNLVFED EITALQPEVD KLKTLNVNKI IALGHSGFEM DKLIAQKVRG VDVVVGGHSN TFLYTGN.

    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.

    Nt5E Cd73 Human
  • View Data Sheet

    Description:

    Tissue Inhibitor of Metalloprotease 1 Human Recombinant, Sf9

    TIMP Metallopeptidase Inhibitor 1, TIMP, EPA, Tissue Inhibitor Of Metalloproteinases 1, Fibroblast Collagenase Inhibitor, Erythroid-Potentiating Activity, Collagenase Inhibitor, TIMP-1, CLGI, Tissue Inhibitor Of Metalloproteinase 1 (Erythroid Potentiating Activity, Collagenase Inhibitor), Erythroid Potentiating Activity, Metalloproteinase Inhibitor 1, EPO, HCI, Metalloproteinase inhibitor 1.

    Product # :

    ENZ-876

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    Description

    TIMP1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 190 amino acids (24-207a.a.) and having a molecular mass of 21.5kDa. TIMP1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    TIMP1 protein solution (0.2mg/ml) contains phosphate buffered saline (pH7.4).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      TIMP1 is a member of the TIMP family. TIMP1 is an inducible glycoprotein produced by various cell types. The TIMP1 glycoprotein is a natural inhibitor of the matrix metalloproteinases, which a group of peptidases involved in degradation of the extracellular matrix. TIMP1 binds in a reversible mode to MMPs, with regions in the N-terminal domain binding to the MMP substrate-binding site. On top of its inhibitory function against most of the known MMPs, TIMP1 is able to promote cell proliferation in a broad range of cell types, and may also have an anti-apoptotic role. Furthermore, TIMP1 has erthyroid-potentiating activity via translocation to the nucleus and also inhibits apoptosis in B-cells. The TIMP1 gene is situated within intron 6 of the synapsin I gene and is transcribed in the opposite direction. TIMP1 activity is dependent on the existence of disulfide bonds. TIMP1 transcription is extremely inducible in reaction to many cytokines and hormones.
      Increased TIMP1 levels are connected with squamous cell laryngeal carcinoma. TIMP1 overexpression is linked to gastric cancer.

    • Synonyms

      TIMP Metallopeptidase Inhibitor 1, TIMP, EPA, Tissue Inhibitor Of Metalloproteinases 1, Fibroblast Collagenase Inhibitor, Erythroid-Potentiating Activity, Collagenase Inhibitor, TIMP-1, CLGI, Tissue Inhibitor Of Metalloproteinase 1 (Erythroid Potentiating Activity, Collagenase Inhibitor), Erythroid Potentiating Activity, Metalloproteinase Inhibitor 1, EPO, HCI, Metalloproteinase inhibitor 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. Please avoid freeze thaw cycles.

    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.

    Timp1 Human Sf9
  • View Data Sheet

    Description:

    Bone Morphogenetic protein-3 Human Recombinant

    Bone Morphogenetic Protein 3, Osteogenin, Bone Morphogenetic Protein 3 (Osteogenic), Bone Morphogenetic Protein 3A, BMP-3A, BMP-3, Bone Morphogenetic Protein-3, BMP3A, BMP3.

    Product # :

    CYT-937

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    Description

    BMP3 Human Recombinant produced in E.coli is a non-glycosylated disulfide linked homodimer containing 2 chains of 110 amino acids and having a molecular mass of 24.8kDa.The BMP-3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    BMP-3 protein was lyophilized from a 0.2µm filtered concentrated solution in 30% Acetonitrile and 0.1% TFA.

    Purity

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

    Biological Activity

    The ED50 as determined by its ability to inhibit BMP-2-induced activity in murine MC3T3- E1 cells.

    More Info

    • Introduction

      Bone Morphogenetic Protein 3 (BMP3) is one of the BMPs, some of which are members of the TGF-beta superfamily (BMP2-7). There are more than 13 BMPs, which are involved in inducing cartilage and bone formation, embryogenesis and morphogenesis of various tissues and organs. In addition, BMPs regulate the growth, differentiation, chemotaxis, and apoptosis of various cell types. Akin to most other TGF-beta family proteins, BMPs are extremely conserved across animal species. At the amino acid sequence level, mature human and rat BMP3 are 98% identical.

    • Synonyms

      Bone Morphogenetic Protein 3, Osteogenin, Bone Morphogenetic Protein 3 (Osteogenic), Bone Morphogenetic Protein 3A, BMP-3A, BMP-3, Bone Morphogenetic Protein-3, BMP3A, BMP3.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized BMP3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BMP-3 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 BMP3 in sterile 4mM HCl not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      QWIEPRNCAR RYLKVDFADI GWSEWIISPK SFDAYYCSGA CQFPMPKSLK PSNHATIQSI VRAVGVVPGI PEPCCVPEKM SSLSILFFDE NKNVVLKVYP NMTVESCACR.

    • Background

      Bone Morphogenetic Protein-3 Human Recombinant: Unveiling the Potential of a Key Regulator in Tissue Regeneration

      Abstract:

      Bone Morphogenetic Protein-3 (BMP-3) human recombinant is a critical member of the bone morphogenetic protein family, known for its role in tissue development, repair, and regeneration. This research paper provides a comprehensive analysis of BMP-3, including its characteristics, signaling pathways, and potential therapeutic applications. Additionally, innovative methodologies for the production and optimization of BMP-3 human recombinant are proposed, shedding light on its future implications in the field of regenerative medicine.

      Introduction:

      Tissue regeneration is a complex biological process requiring precise molecular cues. BMP-3, a crucial member of the BMP family, plays a significant role in tissue development and regeneration. This paper explores the unique features of BMP-3 and presents novel approaches for its production and optimization, aiming to unlock its therapeutic potential in various regenerative contexts.

      Characteristics and Signaling Pathways:

      BMP-3 is a secreted protein that binds to cell surface receptors, initiating intracellular signaling cascades. It influences cell differentiation, proliferation, and extracellular matrix synthesis through both Smad-dependent and Smad-independent signaling pathways. BMP-3 signaling regulates critical processes involved in tissue regeneration, including chondrogenesis and osteogenesis.

      Production of BMP-3 Human Recombinant:

      Efficient production methodologies are essential for harnessing the therapeutic potential of BMP-3 human recombinant. Recombinant protein expression systems, such as Escherichia coli or mammalian cells, have been utilized to produce functional BMP-3. Optimization strategies, including codon optimization, signal peptide engineering, and protein folding optimization, have been employed to enhance the yield and activity of BMP-3 recombinant protein.

      Potential Therapeutic Applications:

      BMP-3 human recombinant holds significant promise in the field of regenerative medicine. It plays a crucial role in bone and cartilage regeneration, making it a potential candidate for the treatment of skeletal disorders and tissue injuries. Additionally, BMP-3 signaling influences tissue remodeling and wound healing, suggesting its broader therapeutic applications in other regenerative processes.

      Conclusion:

      BMP-3 human recombinant represents a key regulator in tissue regeneration, with immense potential in regenerative medicine. Optimizing production methodologies and further unraveling its signaling mechanisms will enhance its therapeutic applications. With its implications in bone and cartilage regeneration and its role in tissue remodeling, BMP-3 human recombinant emerges as a promising tool for promoting tissue repair and regeneration.

      What is the molecular weight/Mw of BMP3 Protein?
      BMP3 Protein has a total Mw of 24.8kDa.

      What is the source or expression system of BMP3 Protein?
      Escherichia Coli.

      What is the Purity of BMP3 Protein?
      BMP3 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of BMP3 Protein?
      The ED50 as determined by its ability to inhibit BMP-2-induced activity in murine MC3T3- E1 cells.

      What is the amino acid sequence of BMP3 Protein?
      QWIEPRNCAR RYLKVDFADI GWSEWIISPK SFDAYYCSGA CQFPMPKSLK PSNHATIQSI VRAVGVVPGI PEPCCVPEKM SSLSILFFDE NKNVVLKVYP NMTVESCACR.

      What applications can BMP3 Protein be used in?
      BMP3 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for BMP3 Protein?
      The endotoxin level is minimal, BMP3 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.

    Bmp3 Human
  • View Data Sheet

    Description:

    CD276 Human Recombinant

    CD276 Molecule, CD276 Antigen, Costimulatory Molecule, B7 Homolog 3, 4Ig-B7-H3, B7-H3, B7H3, B7RP-2.

    Product # :

    PRO-2456

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    Description

    CD276 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 446 amino acids (29-466a.a.) and having a molecular mass of 48.1kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa). CD276 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    CD276 protein solution (0.5mg/ml) contains Phosphate buffered saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CD276, belongs to the B7 family of immunoregulatory transmembrane glycoproteins expressed by T cells. CD276 is a costimulatory molecule for T cell activation in addition to IFN-gamma production. Furthermore CD276 upregulates BRCC3 expression, preventing DNA defects caused by 5-Fu. CD276 is correlated with TNM stage of NSCLC and act as a potential biomarker for NSCLC-derived MPEs. CD276 inhibits natural-killer mediated cell lysis in tumor cells, and act as a marker for detection of neuroblastoma cells. CD276 is implicated in the development of acute as well as chronic transplant rejection and in the regulation of lymphocytic activity at mucosal surfaces. In addition, CD276 provides the placenta & fetus a proper immunological environment during the course of pregnancy.

    • Synonyms

      CD276 Molecule, CD276 Antigen, Costimulatory Molecule, B7 Homolog 3, 4Ig-B7-H3, B7-H3, B7H3, B7RP-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

      LEVQVPEDPV VALVGTDATL CCSFSPEPGF SLAQLNLIWQ LTDTKQLVHS FAEGQDQGSA YANRTALFPD LLAQGNASLR LQRVRVADEG SFTCFVSIRD FGSAAVSLQV AAPYSKPSMT LEPNKDLRPG DTVTITCSSY QGYPEAEVFW QDGQGVPLTG NVTTSQMANE QGLFDVHSIL RVVLGANGTY SCLVRNPVLQ QDAHSSVTIT PQRSPTGAVE VQVPEDPVVA LVGTDATLRC SFSPEPGFSL AQLNLIWQLT DTKQLVHSFT EGRDQGSAYA NRTALFPDLL AQGNASLRLQ RVRVADEGSF TCFVSIRDFG SAAVSLQVAA PYSKPSMTLE PNKDLRPGDT VTITCSSYRG YPEAEVFWQD GQGVPLTGNV TTSQMANEQG LFDVHSVLRV VLGANGTYSC LVRNPVLQQD AHGSVTITGQ PMTFPPEALE HHHHHH.

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    Cd276 Human
  • View Data Sheet

    Description:

    Mouse Anti Human Natural Cytotoxicity Triggering Receptor 3

    Natural Cytotoxicity Triggering Receptor 3, LY117, 1C7, Lymphocyte Antigen 117, Activating Natural Killer Receptor P30, Natural Killer Cell P30-Related Protein, NK-p30, NKp30, CD337, MALS, Activating NK-A1 Receptor, CD337 Antigen, NKP30.

    Product # :

    ANT-740

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    Formulation

    1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.

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    • Introduction

      Cytotoxicity Triggering Receptor 3 also known as NCR3 is a natural cytotoxicity receptor (NCR) which assists NK cells in the lysis of tumor cells. Moreover, NCR3 interacts with CD3-zeta (CD247), a T-cell receptor. A single nucleotide polymorphism in the 5' untranslated region of NCR3 has been related with mild malaria suceptibility. Three transcript variants encoding various isoforms have been found for this gene.

    • Synonyms

      Natural Cytotoxicity Triggering Receptor 3, LY117, 1C7, Lymphocyte Antigen 117, Activating Natural Killer Receptor P30, Natural Killer Cell P30-Related Protein, NK-p30, NKp30, CD337, MALS, Activating NK-A1 Receptor, CD337 Antigen, NKP30.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Anti-human NCR3 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human NCR3 protein 19-138 amino acids purified from E. coli.

    • Ig Subclass

      Mouse IgG1 heavy chain and k light chain.

    • Clone

      PAT38D9AT.

    • Applications

      NCR3 antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

      For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.

    • Purification Method

      NCR3 antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.

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

    Ncr3 Antibody
  • View Data Sheet

    Description:

    Mitogen-Activated Protein Kinase 10 Human Recombinant

    C-Jun N-Terminal Kinase 3, MAP Kinase P49 3F12, MAP Kinase 10, PRKM10, SAPK1b, JNK3A, JNK3.

    Product # :

    PKA-115

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    Description

    MAPK10 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 470 amino acids (1-464 a.a.) and having a molecular mass of 53.4kDa. MAPK10 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    MAPK10 is protein solution ( 0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4), 30% glycerol, 1mM DTT and 0.1mM PMSF.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

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    • Introduction

      MAPK10 is part of the MAP kinase protein family. MAP Kinases perform as assimilation point for many biochemical pathways. The enzyme also takes part in wide range of cellular pathways: differentiation, proliferation, development and transcription regulation.

    • Synonyms

      C-Jun N-Terminal Kinase 3, MAP Kinase P49 3F12, MAP Kinase 10, PRKM10, SAPK1b, JNK3A, JNK3.

    • 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

      MSLHFLYYCS EPTLDVKIAF CQGFDKQVDV SYIAKHYNMS KSKVDNQFYS VEVGDSTFTV LKRYQNLKPI GSGAQGIVCA AYDAVLDRNV AIKKLSRPFQ NQTHAKRAYR ELVLMKCVNH KNIISLLNVF TPQKTLEEFQ DVYLVMELMD ANLCQVIQME LDHERMSYLL YQMLCGIKHL HSAGIIHRDL KPSNIVVKSD CTLKILDFGL ARTAGTSFMM TPYVVTRYYR APEVILGMGY KENVDIWSVG CIMGEMVRHK ILFPGRDYID QWNKVIEQLG TPCPEFMKKL QPTVRNYVEN RPKYAGLTFP KLFPDSLFPA DSEHNKLKAS QARDLLSKML VIDPAKRISV DDALQHPYIN VWYDPAEVEA PPPQIYDKQL DEREHTIEEW KELIYKEVMN SEEKTKNGVV KGQPSPSGAA VNSSESLPPS SSVNDISSMS TDQTLASDTD SSLEASAGPL GCCRHHHHHH.

    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.

    Mapk10 Human
  • View Data Sheet

    Description:

    Syntaxin-1A Human Recombinant

    STX1, HPC-1, p35-1, Syntaxin-1A, Neuron-specific antigen HPC-1, STX-1A, STX1A.

    Product # :

    PRO-574

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    Description

    Syntaxin-1A Human Recombinant fused to N-terminal His-Tag produced in E.Coli is a single, non-glycosylated polypeptide chain containing 226 amino acids (1-226) and having a molecular mass of 26.1 kDa.Recombinant Human STX1A contains N-terminal domain (Habc) and t_SNARE domain (H3 domain).

    Source

    Escherichia Coli.

    Formulation

    The protein solution contains 20mM Tris-HCl pH7.5, 10% glycerol, and 1mM DTT.

    Purity

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

    More Info

    • Introduction

      Syntaxin is membrane integrated Q-SNARE protein participating in exocytosis. Syntaxin is composed of an N-terminal regulatory domain (Habc), a SNARE domain (known as H3), and a single C-terminal transmembrane domain. The SNARE (H3) domain binds to both synaptobrevin and SNAP-25 forming the core SNARE complex. Synaptic vesicles store neurotransmitters that are released during calcium-regulated exocytosis. The specificity of neurotransmitter release requires the localization of both synaptic vesicles and calcium channels to the presynaptic active zone. Syntaxins function in this vesicle fusion process. Syntaxins also serve as a substrate for botulinum neurotoxin type C, a metalloprotease that blocks exocytosis and has high affinity for a molecular complex that includes the alpha-latrotoxin receptor which produces exocytosis.

    • Synonyms

      STX1, HPC-1, p35-1, Syntaxin-1A, Neuron-specific antigen HPC-1, STX-1A, STX1A.

    • 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

      MKDRTQELRT AKDSDDDDDV AVTVDRDRFM DEFFEQVEEI RGFIDKIAEN VEEVKRKHSA ILASPNPDEK TKEELEELMS DIKKTANKVR SKLKSIEQSI EQEEGLNRSS ADLRIRKTQH STLSRKFVEV MSEYNATQSD YRERCKGRIQ RQLEITGRTT TSEELEDMLE SGNPAIFASG IIMDSSISKQ ALSEIETRHS EIIKLENSIR ELHDMFMDMA MLVESQ.

    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.

    Stx1A Human
  • View Data Sheet

    Description:

    Interleukin-2 Mouse Recombinant

    Interleukin-2, T-cell growth factor (TCGF),  Lymphokine, IL-2.

    Product # :

    CYT-370

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    Description

    Interleukin-2 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 148 amino acids and having a molecular mass of 17.2kDa. The IL-2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution (1mg/ml) in 20mM PBS, pH 7.4.

    Purity

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

    Biological Activity

    The ED50 as determined by the dose-dependant stimulation of murine CTLL-2 cells is less than 0.2ng/ml corresponding to a Specific Activity of 5x106IU/mg.

    More Info

    • Introduction

      IL2 is a secreted cytokine that is important for the proliferation of T and B lymphocytes. The receptor of this cytokine is a heterotrimeric protein complex whose gamma chain is also shared by interleukin 4 (IL4) and interleukin 7 (IL7). The expression of this gene in mature thymocytes is monoallelic, which represents an unusual regulatory mode for controlling the precise expression of a single gene. The targeted disruption of a similar gene in mice leads to ulcerative colitis-like disease, which suggests an essential role of this gene in the immune response to antigenic stimuli.

    • Synonyms

      Interleukin-2, T-cell growth factor (TCGF), Lymphokine, IL-2.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Interleukin-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL2 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 Mouse IL-2 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      PTSSSTSSST AEAQQQQQQQ QQQQQHLEQL LMDLQELLSR MENYRNLKLP RMLTFKFYLP KQATELKDLQ CLEDELGPLR HVLDLTQSKS FQLEDAENFI SNIRVTVVKL KGSDNTFECQ FDDESATVVD FLRRWIAFCQ SIISTSPQ.

    • Background

      What is the molecular weight/Mw of IL 2 MOUSE Protein?
      IL 2 MOUSE Protein has a total Mw of 17.2kDa.

      What is the source or expression system of IL 2 MOUSE Protein?
      Escherichia Coli.

      What is the Purity of IL 2 MOUSE Protein?
      IL 2 MOUSE Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL 2 MOUSE Protein?
      The ED50 as determined by the dose-dependant stimulation of murine CTLL-2 cells is less than 0.2ng/ml corresponding to a Specific Activity of 5x106IU/mg.

      What is the amino acid sequence of IL 2 MOUSE Protein?
      PTSSSTSSST AEAQQQQQQQ QQQQQHLEQL LMDLQELLSR MENYRNLKLP RMLTFKFYLP KQATELKDLQ CLEDELGPLR HVLDLTQSKS FQLEDAENFI SNIRVTVVKL KGSDNTFECQ FDDESATVVD FLRRWIAFCQ SIISTSPQ.

      What applications can IL 2 MOUSE Protein be used in?
      IL 2 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IL 2 MOUSE Protein?
      The endotoxin level is minimal, IL 2 MOUSE Protein was purified using conventional chromatography techniques.

      Who supplies recombinant IL 2 MOUSE that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of IL 2 MOUSE?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

    • Protein content

      Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.482 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a calibrated solution of IL-2 as a Reference Standard.

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

    Il 2 Mouse
  • View Data Sheet

    Description:

    B-Cell Lymphoma Protein 2 Alpha Human Recombinant, His Tag

    Apoptosis regulator Bcl-2, BCL2, B-cell CLL/lymphoma 2, Bcl-2.

    Product # :

    PRO-683

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    Description

    BCL2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing amino acids 1-211 and having a molecular mass of 25.4 kDa. The BCL2 is fused to a 20 a.a. His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The BCL2 protein solution contains 20mM Tris-HCl, pH-8, 2mM DTT and 20% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      BCL2 gene encodes an integral outer mitochondrial membrane protein that blocks the apoptotic death of some cells such as lymphocytes. Constitutive expression of BCL2, such as in the case of translocation of BCL2 to Ig heavy chain locus, is thought to be the cause of follicular lymphoma. Two transcript variants, produced by alternate splicing, differ in their C-terminal ends.

    • Synonyms

      Apoptosis regulator Bcl-2, BCL2, B-cell CLL/lymphoma 2, Bcl-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 MAHAGRTGYD NREIVMKYIH YKLSQRGYEW DAGDVGAAPP GAAPAPGIFS SQPGHTPHPA ASRDPVARTS PLQTPAAPGA AAGPALSPVP PVVHLTLRQA GDDFSRRYRR DFAEMSSQLH LTPFTARGRF ATVVEELFRD GVNWGRIVAF FEFGGVMCVE SVNREMSPLV DNIALWMTEY LNRHLHTWIQ DNGGWDAFVE LYGPSMRPLF D.

    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.

    Bcl2 Human His
  • View Data Sheet

    Name :

    IL7 Rat

    Description:

    Interleukin-7 Rat Recombinant

    Lymphopoietin 1 (LP-1), pre-B cell factor, IL-7.

    Product # :

    CYT-163

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    Description

    IL 7 Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 129 amino acids and having a molecular mass of 15.0kDa.The IL 7 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 98.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 was determined by the dose-dependent stimulation of the proliferation of murine 2E8 cells is less than 0.2ng/ml, corresponding to a specific activity of >5,000,000IU/mg.

    More Info

    • Introduction

      IL-7 is a cytokine important for B and T cell development. This cytokine and the hepatocyte growth factor (HGF) form a heterodimer that functions as a pre-pro-B cell growth-stimulating factor. This cytokine is found to be a cofactor for V(D)J rearrangement of the T cell receptor beta (TCRB) during early T cell development. This cytokine can be produced locally by intestinal epithelial and epithelial goblet cells, and may serve as a regulatory factor for intestinal mucosal lymphocytes. Knockout studies in mice suggested that this cytokine plays an essential role in lymphoid cell survival.

    • Synonyms

      Lymphopoietin 1 (LP-1), pre-B cell factor, IL-7.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IL-7 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL-7 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 IL-7 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      DCHIKDKDGK AFGSVLMISI NQLDKMTGTD SDCPNNEPNF FKKHLCDDTK EAAFLNRAAR KLRQFLKMNI SEEFNDHLLR VSDGTQTLVN CTSKEEKTIK EQKKNDPCFL KRLLREIKTC WNKILKGSI

    • Background

      What is the molecular weight/Mw of IL7 RAT Protein?
      IL7 RAT Protein has a total Mw of 15kDa.

      What is the source or expression system of IL7 RAT Protein?
      Escherichia Coli.

      What is the Purity of IL7 RAT Protein?
      IL7 RAT Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL7 RAT Protein?
      The ED50 was determined by the dose-dependent stimulation of the proliferation of murine 2E8 cells is less than 0.2ng/ml, corresponding to a specific activity of >5,000,000IU/mg.

      What is the amino acid sequence of IL7 RAT Protein?
      DCHIKDKDGK AFGSVLMISI NQLDKMTGTD SDCPNNEPNF FKKHLCDDTK EAAFLNRAAR KLRQFLKMNI SEEFNDHLLR VSDGTQTLVN CTSKEEKTIK EQKKNDPCFL KRLLREIKTC WNKILKGSI.

      What applications can IL7 RAT Protein be used in?
      IL7 RAT Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IL7 RAT Protein?
      The endotoxin level is minimal, IL7 RAT Protein was purified using conventional chromatography techniques.

      Who supplies recombinant IL7 RAT that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of IL7 RAT?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

    Il 7 Rat
  • View Data Sheet

    Description:

    Interleukin-7 Human Recombinant, HEK

    Lymphopoietin 1 (LP-1), pre-B cell factor, IL-7.

    Product # :

    CYT-197

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    Description

    IL-7 Human Recombinant produced in HEK cells is a glycosylated monomer, having a molecular weight range of 19-30kDa due to glycosylation.The IL-7 is purified by proprietary chromatographic techniques.

    Source

    HEK.

    Formulation

    The IL7 was lyophilized from 1mg/ml in 1xPBS.

    Purity

    Greater than 95% as obsereved by SDS-PAGE.

    Biological Activity

    The activity was determined by the dose dependent stimulation of the proliferation of murine 2E8 cells and is typically 0.3ng/ml corresponding to a specific activity of 3,333,334units/mg.

    More Info

    • Introduction

      IL-7 is a cytokine important for B and T cell development. This cytokine and the hepatocyte growth factor (HGF) form a heterodimer that functions as a pre-pro-B cell growth-stimulating factor. This cytokine is found to be a cofactor for V(D)J rearrangement of the T cell receptor beta (TCRB) during early T cell development. This cytokine can be produced locally by intestinal epithelial and epithelial goblet cells, and may serve as a regulatory factor for intestinal mucosal lymphocytes. Knockout studies in mice suggested that this cytokine plays an essential role in lymphoid cell survival.

    • Synonyms

      Lymphopoietin 1 (LP-1), pre-B cell factor, IL-7.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IL-7 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL7 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 IL-7 in sterile PBS containing 0.1% endotoxin-free recombinant HSA.

    • Background

      What is the molecular weight/Mw of IL7 HUMAN, HEK Protein?
      IL7 HUMAN, HEK Protein has a total Mw of 24.5kDa.

      What is the source or expression system of IL7 HUMAN, HEK Protein?
      HEK.
      What is the Purity of IL7 HUMAN, HEK Protein?
      IL7 HUMAN, HEK Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL7 HUMAN, HEK Protein?
      The activity was determined by the dose dependent stimulation of the proliferation of murine 2E8 cells and is typically 0.3ng/ml corresponding to a specific activity of 3,333,334units/mg.

      What applications can IL7 HUMAN, HEK Protein be used in?
      IL7 HUMAN, HEK Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IL7 HUMAN, HEK Protein?
      The endotoxin level is minimal, IL7 HUMAN, HEK Protein was purified using conventional chromatography techniques.

      Who supplies recombinant IL7 HUMAN, HEK that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of IL7 HUMAN, HEK?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

    Il 7 Human Hek
  • View Data Sheet

    Description:

    BCL2 Like 2 Human Recombinant

    B-Cell Lymphoma Protein 2, BCL2 Like 2, BCL2 Like protein 2, BCLW, Bcl2-L-2, Apoptosis regulator Bcl-W, BCL2L2, BCL-W, KIAA0271.

    Product # :

    PRO-1577

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    Description

    Recombinant Human BCL2L2 produced in E.coli cells is a non-glycosylated, homodimeric protein containing 171 amino acid chain and having a molecular mass of 18.6kDa. The Human BCL2L2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    BCL2L2 is a 0.2µm filtered concentrated solution which contains 25 mM Hepes, pH 7.4, 100 mM KCl, 10 % Glycerol, 5 % Trehalose, and 0.02 % Tween-80.

    Purity

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

    More Info

    • Introduction

      BCL2L2 promotes cell survival. BCL2L2 mediates survival of postmitotic Sertoli cells by suppressing death-promoting activity of BAX. BCL2L2 is part of the BCL-2 protein family which form hetero- or homodimers and play an important role as anti and proapoptotic regulators. BCL2L2 causes reduced cell apoptosis under cytotoxic conditions. BCL2L2 is involved in the survival of NGF- and BDNF-dependent neurons. BCL2L2 plays an important role in adult spermatogenesis.

    • Synonyms

      B-Cell Lymphoma Protein 2, BCL2 Like 2, BCL2 Like protein 2, BCLW, Bcl2-L-2, Apoptosis regulator Bcl-W, BCL2L2, BCL-W, KIAA0271.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      BCL2L2 although stable at room temperature for 3 weeks, should be stored at 4°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).

    • Amino Acid Sequence

      ATPASAPDTR ALVADFVGYK LRQKGYVCGA GPGEGPAADP LHQAMRAAGD EFETRFRRTF SDLAAQLHVT PGSAQQRFTQ VSDELFQGGP NWGRLVAFFV FGAALCAESV NKEMEPLVGQ VQEWMVAYLE TQLADWIHSS GGWAEFTALY GDGALEEARR LREGNWASVR T

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    Human Bcl2L2
  • View Data Sheet

    Description:

    Cytokeratin 8 Human Recombinant, His Tag

    Keratin type II cytoskeletal 8, Cytokeratin-8, CK-8, Keratin-8, K8, KRT8, CYK8, KO, CK8, K2C8, CARD2.

    Product # :

    PRO-1567

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    Description

    KRT8 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 506 amino acids (1-483 a.a) and having a molecular mass of 56kDa. KRT8 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    KRT8 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Cytokeratin 8 (KRT8) belongs to the type II keratin family clustered on the long arm of chromosome 12. Type I and type II keratins heteropolymerize to form intermediate-sized filaments in the cytoplasm of epithelial cells. KRT8 typically dimerizes with keratin 18 to form an intermediate filament in simple single-layered epithelial cells. KRT8 has a role in retaining cellular structural integrity and also functions in signal transduction and cellular differentiation. KRT8 gene mutations cause cryptogenic cirrhosis.

    • Synonyms

      Keratin type II cytoskeletal 8, Cytokeratin-8, CK-8, Keratin-8, K8, KRT8, CYK8, KO, CK8, K2C8, CARD2.

    • 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 MGSMSIRVTQ KSYKVSTSGP RAFSSRSYTS GPGSRISSSS FSRVGSSNFR GGLGGGYGGA SGMGGITAVT VNQSLLSPLV LEVDPNIQAV RTQEKEQIKT LNNKFASFID KVRFLEQQNK MLETKWSLLQ QQKTARSNMD NMFESYINNL RRQLETLGQE KLKLEAELGN MQGLVEDFKN KYEDEINKRT EMENEFVLIK KDVDEAYMNK VELESRLEGL TDEINFLRQL YEEEIRELQS QISDTSVVLS MDNSRSLDMD SIIAEVKAQY EDIANRSRAE AESMYQIKYE ELQSLAGKHG DDLRRTKTEI SEMNRNISRL QAEIEGLKGQ RASLEAAIAD AEQRGELAIK DANAKLSELE AALQRAKQDM ARQLREYQEL MNVKLALDIE IATYRKLLEG EESRLESGMQ NMSIHTKTTS GYAGGLSSAY GGLTSPGLSY SLGSSFGSGA GSSSFSRTSS SRAVVVKKIE TRDGKLVSES SDVLPK.

    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.

    Krt8 Human His