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Search results

1000 results found for “Cyclin”

Name

Description

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  • View Data Sheet

    Name :

    CD79B Human, Sf9

    Description:

    CD79B Human Recombinant, Sf9

    CD79b Molecule, CD79B Antigen (Immunoglobulin-Associated Beta), CD79b Molecule, Immunoglobulin-Associated Beta, Immunoglobulin-Associated B29 Protein, B-Cell-Specific Glycoprotein B29, Ig-Beta, IGB, B29, B-Cell Antigen Receptor Complex-Associated Protein Beta Chain, CD79b Antigen, CD79B, AGM6.

    Product # :

    PRO-2404

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    Description

    CD79B Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 140 amino acids (29-159a.a.) and having a molecular mass of 16.3kDa (Molecular size on SDS-PAGE will appear at approximately 18-28 kDa).CD79B is expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    CD79B protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CD79B is a 36 kDa trans membrane glycoprotein belonging to the immunoglobulin superfamily. Heterodimers of CD79A and CD79B connect with a membrane attached immunoglobulin on the B cell surface to create the B cell antigen receptor complex (BCR). CD79A and CD79B are essential for BCR-mediated signaling and subsequently for the development and activation of B lineage cells.

    • Synonyms

      CD79b Molecule, CD79B Antigen (Immunoglobulin-Associated Beta), CD79b Molecule, Immunoglobulin-Associated Beta, Immunoglobulin-Associated B29 Protein, B-Cell-Specific Glycoprotein B29, Ig-Beta, IGB, B29, B-Cell Antigen Receptor Complex-Associated Protein Beta Chain, CD79b Antigen, CD79B, AGM6.

    • 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

      ADPARSEDRY RNPKGSACSR IWQSPRFIAR KRGFTVKMHC YMNSASGNVS WLWKQEMDEN PQQLKLEKGR MEESQNESLA TLTIQGIRFE DNGIYFCQQK CNNTSEVYQG CGTELRVMGF STLAQLKQRN TLKDHHHHHH.

    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.

    Cd79B Human Sf9
  • View Data Sheet

    Name :

    RHOC Human

    Description:

    Ras Homolog Gene Family Member C Human Recombinant

    ARH9, ARHC, H9, RHOH9, RAS-related homolog 9, Rho cDNA clone 9, Rho-related GTP-binding protein RhoC, ARH9, MGC1448, MGC61427, RHOC.

    Product # :

    PRO-865

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    Description

    RHOC Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 210 amino acids (1-190 a.a.) and having a molecular mass of 23.8 kDa. The RHOC is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    RHOC Human 0.5mg/ml solution containing 20mM Tris-HCl pH-8, 0.1M NaCl, 1mM DTT & 20% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      RHOC is a small signaling G protein/GTPase which is part of the Rac subfamily of the family Rho family of GTPases. RHOC rotats between inactive GDP-bound and active GTP-bound states and has a role as a molecular switch in signal transduction cascades. RHOC promotes reorganization of the actin cytoskeleton and regulates cell shape, attachment, and motility.

    • Synonyms

      ARH9, ARHC, H9, RHOH9, RAS-related homolog 9, Rho cDNA clone 9, Rho-related GTP-binding protein RhoC, ARH9, MGC1448, MGC61427, RHOC.

    • 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 MAAIRKKLVI VGDGACGKTC LLIVFSKDQF PEVYVPTVFE NYIADIEVDG KQVELALWDT AGQEDYDRLR PLSYPDTDVI LMCFSIDSPD SLENIPEKWT PEVKHFCPNV PIILVGNKKD LRQDEHTRRE LAKMKQEPVR SEEGRDMANR ISAFGYLECS AKTKEGVREV FEMATRAGLQ VRKNKRRRGC.

    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.

    Rhoc Human
  • View Data Sheet

    Name :

    CRYAB Human, His

    Description:

    Crystallin Alpha B Human Recombinant, His Tag

    CRYA2, CTPP2, HSPB5, Crystallin Alpha B, CRYAB.

    Product # :

    HSP-088

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    Description

    CRYAB Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 183 amino acids (1-175) and having a molecular mass of 21.2kDa. CRYAB is fused to an 8 a.a his-Tag at C-terminus and is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CRYAB solution (1mg/ml) contains 10% glycerol & Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Synonyms

      CRYA2, CTPP2, HSPB5, Crystallin Alpha B, CRYAB.

    • 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

      MDIAIHHPWI RRPFFPFHSP SRLFDQFFGE HLLESDLFPT STSLSPFYLR PPSFLRAPSW FDTGLSEMRL EKDRFSVNLD VKHFSPEELK VKVLGDVIEV HGKHEERQDE HGFISREFHR KYRIPADVDP LTITSSLSSD GVLTVNGPRK QVSGPERTIP ITREEKPAVT AAPKKLEHHH HHH.

    • Background

      Alpha-B crystallin (CRYAB), a small heat shock protein, stands as a multifaceted molecular chaperone integral to cellular homeostasis and stress response. In its human recombinant form, CRYAB becomes a focal point in biomedical research, offering a controlled platform to explore its structural intricacies, cellular functions, and potential therapeutic applications. This research embarks on a comprehensive journey to unveil the diverse roles of CRYAB Human Recombinant, shedding light on its structural attributes, cellular interactions, and its implications in health and disease. By delving into the properties of CRYAB, scientists aim to deepen our understanding of cellular proteostasis and explore novel avenues in the treatment of protein misfolding disorders.

      Structural Insights into CRYAB Human Recombinant:

      CRYAB, forming oligomeric complexes, possesses a dynamic structural configuration crucial for its chaperone function. The human recombinant form, designed for controlled study, provides a unique window into the three-dimensional intricacies of CRYAB. Understanding its structure is fundamental for deciphering how CRYAB engages with client proteins, preventing their aggregation and maintaining cellular proteostasis.

      Cellular Functions in Proteostasis:

      As a molecular chaperone, CRYAB plays a pivotal role in preserving cellular proteostasis by preventing the aggregation of misfolded proteins. Beyond its chaperone function, CRYAB is implicated in diverse cellular processes, including modulation of apoptosis, regulation of cytoskeletal dynamics, and participation in cell signaling pathways. Elucidating the multifaceted functions of CRYAB Human Recombinant provides insights into its roles in health and disease.

      Implications in Neurodegenerative Disorders:

      CRYAB has garnered attention in the context of neurodegenerative disorders, where protein misfolding and aggregation are central pathological features. Studies involving CRYAB Human Recombinant have revealed its neuroprotective properties, suggesting its potential as a therapeutic target for conditions like Alzheimer's and Parkinson's diseases. Understanding the mechanisms by which CRYAB mitigates protein aggregation in neuronal cells holds promise for developing targeted interventions.

      CRYAB in Cardiovascular Health:

      The chaperone function of CRYAB extends to the cardiovascular system, where it safeguards against protein aggregation in cardiomyocytes. CRYAB Human Recombinant studies have illuminated its protective role in cardiac tissues, positioning it as a potential therapeutic avenue for heart diseases characterized by protein misfolding.

      Challenges and Future Directions:

      While the potential of CRYAB Human Recombinant in therapeutics is evident, challenges persist. Fine-tuning its applications, understanding its interactions with diverse client proteins, and exploring the intricacies of its roles in different cellular contexts are critical for translational success. Additionally, deciphering the specific mechanisms by which CRYAB contributes to the alleviation of protein misfolding disorders remains an active area of investigation.

      CRYAB Human Recombinant emerges as a linchpin in the cellular orchestra, orchestrating a symphony of functions vital for proteostasis. Its structural insights, diverse cellular functions, and therapeutic implications position it at the forefront of biomedical research. As researchers continue to unravel the molecular nuances of CRYAB, they not only deepen our understanding of cellular proteostasis but also pave the way for innovative treatments in neurodegenerative and cardiovascular disorders, shaping the future of precision medicine and protein folding therapeutics.

    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.

    Cryab Human His
  • View Data Sheet

    Name :

    MYL1 Human

    Description:

    Myosin Light Chain 1 Human Recombinant

    Myosin light chain 1 skeletal muscle isoform, MLC1F, A1 catalytic, Alkali myosin light chain 1, MYL1, MLC3F.

    Product # :

    PRO-365

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    Description

    Recombinant Human Ventricular Myosin Light Chain-1 (MYL1) protein has a molecular mass of 25 kDa and is fused to 7 amino acids at N-terminus. The MYL1 protein was affinity purified using anti MYL1 monoclonal antibody 39-15 column.

    Source

    Escherichia Coli.

    Formulation

    Human MYL1 in 10mM Tris -HCI, 1mM EDTA PH 7.5.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Myosin is a hexameric ATPase cellular motor protein, which is composed of 2 heavy chains, 2 non-phosphorylatable alkali light chains, and 2 phosphorylatable regulatory light chains.
      MYL1 gene encodes a myosin alkali light chain expressed in fast skeletal muscle. Two transcript variants have been identified for the MYL1 gene. In humans MYL1 is localized to chromosome 2q32.1-qter. The Myl1 locus encodes two alkali myosin light chains- Mlc1f and Mlc3f, from two promoters that are differentially regulated throughout development. The Mlc1f promoter is active in embryonic, fetal and adult fast skeletal muscle while the Mlc3f promoter is upregulated during fetal development and stays on in adult fast skeletal muscle.

    • Synonyms

      Myosin light chain 1 skeletal muscle isoform, MLC1F, A1 catalytic, Alkali myosin light chain 1, MYL1, MLC3F.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store vial at -20°C to -80°C. When stored at the recommended temperature, this protein is stable for 12 months.Please prevent 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.

    Myl1 Human
  • View Data Sheet

    Name :

    SNX3 Human

    Description:

    Sorting Nexin 3 Human Recombinant

    Sorting nexin-3, Protein SDP3, SNX3, SDP3, Grd19, MCOPS8.

    Product # :

    PRO-246

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    Description

    SNX3 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 182 amino acids (1-162 a.a) and having a molecular mass of 20.9kDa.SNX3 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SNX3 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 20% glycerol and 0.1M NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Sorting nexin 3 (SNX3) belongs to the large family of hydrophilic proteins, which interact with various receptor types and are involved in intracellular trafficking. SNX3 interacts with phosphatidylinositol-3-phosphate, and is involved in protein trafficking. SNX3 comprises a distinct subgroup of nexins, which share less sequence similarity outside of the PX domain and have significantly different binding affinities for the tyrosine kinase receptors.

    • Synonyms

      Sorting nexin-3, Protein SDP3, SNX3, SDP3, Grd19, MCOPS8.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      SNX3 Human Recombinant although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MAETVADTRR LITKPQNLND AYGPPSNFLE IDVSNPQTVG VGRGRFTTYE IRVKTNLPIF KLKESTVRRR YSDFEWLRSE LERESKVVVP PLPGKAFLRQ LPFRGDDGIF DDNFIEERKQ GLEQFINKVA GHPLAQNERC LHMFLQDEII DKSYTPSKIR
      HA.

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    Snx3 Human
  • View Data Sheet

    Name :

    NUCB2 Mouse

    Description:

    Nucleobindin-2 Mouse Recombinant

    Nefa, Calnuc, AI607786, Nucleobindin-2, DNA-binding protein NEFA, Nucb2.

    Product # :

    PRO-605

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    Description

    NUCB2 Mouse Recombinant fused to N-terminal His-Tag produced in E.Coli is a single, non-glycosylated polypeptide chain (amino acids 25-420) containing 417 amino acids and having a molecular mass of 49kDa.NUCB2 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein solution (1mg/ml) contains 20mM Tris-HCl pH-8, 0.1M NaCl and 1mM EDTA.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Nucleobindin-2 (NUCB2) is a EF-hand calcium-binding protein. Nucleobindin-2 takes part in calcium homeostasis and is a multifunctional protein that interacts with Ca(2+) nucleic acids & various regulatory proteins in different signaling pathways. NUCB2 is localized in neuronal perikarya and dendrites of mouse brain.

    • Synonyms

      Nefa, Calnuc, AI607786, Nucleobindin-2, DNA-binding protein NEFA, Nucb2.

    • 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 MVPIDVDKTK VHNTEPVENA RIEPPDTGLY YDEYLKQVIE VLETDPHFRE KLQKADIEEI RSGRLSQELD LVSHKVRTRL DELKRQEVGR LRMLIKAKLD ALQDTGMNHH LLLKQFEHLN HQNPNTFESR DLDMLIKAAT ADLEQYDRTR HEEFKKYEMMKEHERREYLK TLSEEKRKEE ESKFEEMKRK HEDHPKVNHP GSKDQLKEVW EETDGLDPND FDPKTFFKLH DVNNDGFLDE QELEALFTRE LEKVYNPQNA EDDMIEMEEE RLRMREHVMS EIDNNKDRLV TLEEFLRATE KKEFLEPDSW ETLDQQQLFT EDELKEYESI IAIQENELKKRAEELQKQKE DLQRQHDHLE AQKQEYHQAV QHLEQKKLQQ GIAPSGPAGE LKFEPHT.

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    Nucb2 Mouse
  • View Data Sheet

    Name :

    CXCL5 Rat

    Description:

    Epithelial Neutrophil-Activating Protein 78 Rat Recombinant (CXCL5)

    C-X-C motif chemokine 5, Small-inducible cytokine B5, Cytokine LIX, Cxcl5, Scyb5, LIX, GCP-2, Scyb6, ENA-78, AMCF-II.

    Product # :

    CHM-267

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    Description

    Epithelial Neutrophil-Activating Protein 78 Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 93 amino acids and having a molecular mass of 10.0kDa.The CXCL5 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated (1.0mg/ml) solution in 1×PBS, pH 7.4.

    Purity

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

    Biological Activity

    Determined by its ability to chemoattract human 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. 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

      C-X-C motif chemokine 5, Small-inducible cytokine B5, Cytokine LIX, Cxcl5, Scyb5, LIX, GCP-2, Scyb6, ENA-78, AMCF-II.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized ENA-78 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 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      APFSAMVATE LRCVCLTLAP RINPKMIANL EVIPAGPHCP KVEVIAKLKN QKDNVCLDPQ APLIKKVIQK ILGSENKKTK RNALALVRSA STQ.

    • Background

      What is the molecular weight/Mw of CXCL5 RAT Protein?
      CXCL5 RAT Protein has a total Mw of 10.0kDa.

      What is the source or expression system of CXCL5 RAT Protein?
      Escherichia Coli.

      What is the Purity of CXCL5 RAT Protein?
      CXCL5 RAT Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL5 RAT Protein?
      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 RAT Protein?
      APFSAMVATE LRCVCLTLAP RINPKMIANL EVIPAGPHCP KVEVIAKLKN QKDNVCLDPQ APLIKKVIQK ILGSENKKTK RNALALVRSA STQ.

      What applications can CXCL5 RAT Protein be used in?
      CXCL5 RAT Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL5 RAT Protein?
      The endotoxin level is minimal, CXCL5 RAT Protein was purified using conventional chromatography techniques.


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    Ena 78 Rat
  • View Data Sheet

    Name :

    BRK1 Human

    Description:

    BRK1 Human Recombinant

    BRICK1 SCAR/WAVE Actin-Nucleating Complex Subunit, Haematopoietic Stem/Progenitor Cell Protein 300, Homolog (Arabidopsis Thaliana), Chromosome 3 Open Reading Frame 10, Probable Protein BRICK1, BRICK1, HSPC300, MDS027, C3orf10.

    Product # :

    PRO-1836

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    Description

    BRK1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 98 amino acids (1-75) and having a molecular mass of 11.0 kDa. BRK1 is fused to a 23 amino acid His-tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

    The BRK1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 150mM NaCl and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      BRK1 is a member of the BRK1 family. BRK1 takes part in regulating actin and microtubule organization and is a fragment of a WAVE complex which activates the Arp2/3 complex.

    • Synonyms

      BRICK1 SCAR/WAVE Actin-Nucleating Complex Subunit, Haematopoietic Stem/Progenitor Cell Protein 300, Homolog (Arabidopsis Thaliana), Chromosome 3 Open Reading Frame 10, Probable Protein BRICK1, BRICK1, HSPC300, MDS027, C3orf10.

    • 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 MGSMAGQEDP VQREIHQDWA NREYIEIITS SIKKIADFLN SFDMSCRSRL ATLNEKLTAL ERRIEYIEAR VTKGETLT

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    Brk1 Human
  • View Data Sheet

    Name :

    PHB2 Human

    Description:

    Prohibitin 2 Human Recombinant

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

    Product # :

    PRO-1533

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    Description

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

    Source

    Escherichia Coli.

    Formulation

    The PHB2 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

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

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    Phb2 Human
  • View Data Sheet

    Name :

    FKBP3 Human

    Description:

    FK506 Binding Protein 3 Human Recombinant

    EC 5.2.1.8, FKBP-3, FKBP25, FKBP-25, Peptidyl-prolyl cis-trans isomerase FKBP3, PPIase FKBP3, FK506-binding protein 3, Rotamase, Immunophilin FKBP25, 25 kDa FK506-binding protein, 25 kDa FKBP, Rapamycin-selective 25 kDa immunophilin, FKBP3, PPIase.

    Product # :

    ENZ-495

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    Description

    FKBP3 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 224 amino acids (1-224 a.a.) and having a molecular mass of 25.1 kDa. FKBP3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The FKBP3 protein solution contains 20mM Tris-HCl, pH-8, 1mM DTT and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is >900 nmoles/min/mg, and is defined as the amount of enzyme that cleaves 1umole of suc-AAFP-pNA per minute at 37C in Tris-Hcl pH8.0 using chymotrypsin.

    More Info

    • Introduction

      FKBP3 is part of a family of immunosuppressant receptors which inhibit T-cell proliferation by arresting two distinct cytoplasmic signal transmission pathways. FKBP3 accelerates the folding of proteins. FKBP3 is part of the immunophilin protein family, which participates in immunoregulation and fundamental cellular processes concerning protein folding and trafficking. FKBP3 is a cis-trans prolyl isomerase enzyme that binds the immunosuppressants FK506 and rapamycin, as well as histone deacetylases, the transcription factor YY1, casein kinase II, and nucleolin. It has a greater affinity for rapamycin than for FK506 and therefore is a significant protein for immunosuppression by rapamycin.

    • Synonyms

      EC 5.2.1.8, FKBP-3, FKBP25, FKBP-25, Peptidyl-prolyl cis-trans isomerase FKBP3, PPIase FKBP3, FK506-binding protein 3, Rotamase, Immunophilin FKBP25, 25 kDa FK506-binding protein, 25 kDa FKBP, Rapamycin-selective 25 kDa immunophilin, FKBP3, PPIase.

    • 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

      MAAAVPQRAW TVEQLRSEQL PKKDIIKFLQ EHGSDSFLAE HKLLGNIKNV AKTANKDHLV TAYNHLFETK RFKGTESISK VSEQVKNVKL NEDKPKETKS EETLDEGPPK YTKSVLKKGD KTNFPKKGDV VHCWYTGTLQ DGTVFDTNIQ TSAKKKKNAK PLSFKVGVGK VIRGWDEALL TMSKGEKARL EIEPEWAYGK KGQPDAKIPP NAKLTFEVEL VDID.

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    Fkbp3 Human
  • View Data Sheet

    Name :

    PRKACA Human

    Description:

    cAMP-Dependent Protein Kinase A catalytic subunit α Human Recombinant

    cAMP-dependent protein kinase alpha-catalytic subunit, EC 2.7.11.11, PKA C-alpha, PKACA, PRKACA, MGC48865, MGC102831.

    Product # :

    PKA-200

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    Description

    cAMP-dependent PKA is an ubiquitous serine/threonine protein kinase present in a variety of tissues (e.g. brain, skeletal muscle, heart). The intracellular cAMP level regulates cellular responses by altering the interaction between the catalytic C and regulatory R subunits of PKA. The inactive tetrameric PKA holoenzyme R2C2 is activated when cAMP binds to R2, which dissociates the tetramer to R2 cAMP 4 and two active catalytic subunits. Free Catalytic subunits of PKA can phosphorylate a wide variety of intracellular target proteins. In response to hormone- induced high cAMP levels, PKA phosphorylates glycogen synthetase (inhibition of the enzyme activity) and phosphorylase kinase to block glycogen synthesis. Different isoforms of catalytic and regulatory subunits suggest specific functions. The recombinant PKA catalytic subunit a is a 41kDa protein. The a-isoform is the predominant form with a broad tissue distribution and can be used for in vitro enzymological studies of neural and hormonal signal transduction or to phosphorylate target proteins in vivo including Ion channels, transcriptional activator proteins and regulatory enzymes of glycogen metabolism.

    Source

    Escherichia Coli.

    Formulation

    PKA catalytic subunit a is supplied in a buffer containing 20mM MOPS pH7, 150mM NaCl, 1mM DTT, 1mM EDTA and 50% Glycerin.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Synonyms

      cAMP-dependent protein kinase alpha-catalytic subunit, EC 2.7.11.11, PKA C-alpha, PKACA, PRKACA, MGC48865, MGC102831.

    • 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. Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGNAAAAKKG SEQESVKEFL AKAKEDFLKK WESPAQNTAH LDQFERIKTL GTGSFGRVML VKHKETGNHY AMKILDKQKV VKLKQIEHTL NEKRILQAVN FPFLVKLEFS FKDNSNLYMV MEYVPGGEMF SHLRRIGRFS EPHARFYAAQ IVLTFEYLHS LDLIYRDLKP ENLLIDQQGY IQVTDFGFAK RVKGRTWTLC GTPEYLAPEI ILSKGYNKAV DWWALGVLIY EMAAGYPPFF ADQPIQIYEK IVSGKVRFPS HFSSDLKDLL RNLLQVDLTK RFGNLKNGVN DIKNHKWFAT TDWIAIYQRK VEAPFIPKFK GPGDTSNFDD YEEEEIRVSI NEKCGKEFSE F.

    • Assay Conditions

      Roskoski-AssayProtein kinase activity can be measured using a modified radioactive assay according to Roskoski et al.The assay will be performed in a mixture containing 50mM MOPS (pH7.0), 10mM MgCI2, 0.25 mg/ml bovine serum albumin, 100 IJM Kemptide (peptide substrate), 100 IJM unlabeled ATP mixed with [y_32p] ATP (500-1000 cpm/pmol) and Ca subunit in a final volume of 50 IJI. Reaction is started by addition of the Ca subunit and can be stopped after 5 minutes incubation at 30°C by spotting the reaction mix onto Whatman P-81 filters and soaking the filters four times in 75mM phosphoric acid (10 ml per sample) for at least 5 minutes. After four washing steps rinse filters with ethanol, dry and count. Roskoski, R., Jr. (1983) Methods Enzymol. 99, 3-6For the detection of phosphorylation in substrate proteins the phosphotransferase reaction can alternatively be stopped by taking aliquots of the mixture and adding SDS sample buffer. The phosphorylation status of the substrate proteins can subsequently be analysed using SDS PAGE and autoradiography. Zimmermann, B. (1999) Journal of Biological Chemistry.274, 9, 5370-78.

    • Unit Definition

      One unit is defined as the amount of cAMP-Dependent Protein Kinase, recombinant C? catalytic subunit, required to incorporate 1 pmol of phosphate into the specific substrate peptide kemptide (LRRASLG) in one minute at 30°C.

    • Specific Activity

      The specific activity of the recombinant PKA catalytic subunit alpha, is >10,000,000 U/mg.

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    Prkaca
  • View Data Sheet

    Name :

    CFP Human

    Description:

    Complement Factor Properdin Human Recombinant

    Properdin, Complement factor P, CFP, PFC, Complement factor properdin, BFD, PFD, PROPERDIN.

    Product # :

    PRO-2011

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    Description

    CFP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 465 amino acids (28-469 a.a.) and having a molecular mass of 50.9kDa.CFP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CFP protein solution (1mg/ml) containing 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

      Complement Factor Properdin (CFP) which is a plasma glycoprotein, is a positive regulator of the alternative complement pathway of the innate immune system. CFP binds and stabilizes the C3- and C5-convertase enzyme complexes in a feedback loop that eventually ends with formation of the membrane attack complex and lysis of the target cell. Mutations in CFP lead to 2 forms of properdin deficiency that cause high susceptibility to meningococcal infections.

    • Synonyms

      Properdin, Complement factor P, CFP, PFC, Complement factor properdin, BFD, PFD, PROPERDIN.

    • 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 MGSDPVLCFT QYEESSGKCK GLLGGGVSVE DCCLNTAFAY QKRSGGLCQP CRSPRWSLWS TWAPCSVTCS EGSQLRYRRC VGWNGQCSGK VAPGTLEWQL QACEDQQCCP EMGGWSGWGP WEPCSVTCSK GTRTRRRACN HPAPKCGGHC PGQAQESEAC DTQQVCPTHG AWATWGPWTP CSASCHGGPH EPKETRSRKC SAPEPSQKPP GKPCPGLAYE QRRCTGLPPC PVAGGWGPWG PVSPCPVTCG LGQTMEQRTC NHPVPQHGGP FCAGDATRTH ICNTAVPCPV DGEWDSWGEW SPCIRRNMKS ISCQEIPGQQ SRGRTCRGRK FDGHRCAGQQ QDIRHCYSIQ HCPLKGSWSE WSTWGLCMPP CGPNPTRARQ RLCTPLLPKY PPTVSMVEGQ GEKNVTFWGR PLPRCEELQG QKLVVEEKRP CLHVPACKDP EEEEL.

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    Cfp Human
  • View Data Sheet

    Name :

    CHMP2B Human

    Description:

    Chromatin Modifying Protein 2B Human Recombinant

    Chromatin modifying protein 2B, CHMP2.5, VPS2B, Vacuolar protein sorting-associated protein 2-2, hVps2-2, DMT1, DKFZp564O123, VPS2 homolog B.

    Product # :

    PRO-877

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    Description

    CHMP2B Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 233 amino acids (1-213) and having a molecular mass of 26.1 kDa.The CHMP2B is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CHMP2B protein 1mg/ml is supplied in 20mM Tris-HCL, pH-8, 0.1M NaCl, 2mM DTT and 20% Glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CHMP2B is a member of the vacuolar sorting protein family. CHMP2B is a component of the ESCRT-III complex which is essential for sorting endosomal articles into multivesicular bodies (MVBs), and are also obligatory for the formation of these bodies. CHMP2B is usually found in brain, heart, skeletal muscle, small intestine, pancreas, lung, placenta and leukocytes.

    • Synonyms

      Chromatin modifying protein 2B, CHMP2.5, VPS2B, Vacuolar protein sorting-associated protein 2-2, hVps2-2, DMT1, DKFZp564O123, VPS2 homolog B.

    • 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 MASLFKKKTV DDVIKEQNRE LRGTQRAIIR DRAALEKQEK QLELEIKKMA KIGNKEACKV LAKQLVHLRK QKTRTFAVSS KVTSMSTQTK VMNSQMKMAG AMSTTAKTMQ AVNKKMDPQK TLQTMQNFQK ENMKMEMTEE MINDTLDDIF DGSDDEEESQ DIVNQVLDEI GIEISGKMAK APSAARSLPS ASTSKATISD EEIERQLKAL GVD

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    Chmp2B Human
  • View Data Sheet

    Name :

    VAMP5 Human

    Description:

    Vesicle-associated membrane protein 5 Human Recombinant

    VAMP5, Vesicle-associated membrane protein 5, VAMP-5, Myobrevin, HSPC191.

    Product # :

    PRO-681

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    Description

    VAMP5 produced in E.Coli is a single,non-glycosylated polypeptide chain containing 109 amino acids (1-72 a.a.) and having a molecular mass of 12.7 kDa.VAMP5 is fused to 37 amino acids His Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The VAMP5 (0.5mg/ml) protein solution contains 20mM Tris-HCl (pH 8.0), 0.2M NaCl, 5mM DTT, 0.5mM EDTA and 20% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      VAMP5 is part of the vesicle-associated membrane protein (VAMP)/synaptobrevin family and the SNARE superfamily. VAMP5 is involved is vesicle trafficking events that are associated with myogenesis.

    • Synonyms

      VAMP5, Vesicle-associated membrane protein 5, VAMP-5, Myobrevin, HSPC191.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMAG IELERCQQQA NEVTEIMRNN FGKVLERGVK LAELQQRSDQ LLDMSSTFNK TTQNLAQKKC WENIRYRIC.

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    Vamp5 Human
  • View Data Sheet

    Name :

    PTX3 Human

    Description:

    Pentraxin-3 Human Recombinant

    TSG-14, TNFAIP5, PTX3, Pentraxin-related protein PTX3, Pentaxin-related protein PTX3, Tumor necrosis factor-inducible gene 14 protein, TSG14, pentraxin-related gene rapidly induced by IL-1 beta.

    Product # :

    PRO-694

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    Description

    Recombinant Human PTX3 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 401 amino acids (18-381 a.a) and having a molecular mass of 44.4 kDa. PTX3 is fused to a 37 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PTX3 protein contains 20mM Tris-HCl buffer pH-8, 1mM DTT and 10% glycerol.

    Purity

    Greater than 90% as determined by Analysis by SDS-PAGE.

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    • Introduction

      PTX3 is part of the pentraxin family sharing the C-terminal domain with short pentraxins and containing a unique N-terminal domain. PTX3 is produced and released at inflammatory sites by various cell types including monocytes/macrophages, endothelial cells, vascular smooth muscle cells, fibroblasts, and adipocytes. PTX3 is involved in the regulation of innate resistance to pathogens, inflammatory reactions, possibly clearance of self-components and female fertility. PTX3 is used as a marker for disease activity of psoriasis. High serum PTX3 levels are associated with the disease severity of systemic sclerosis. Elevated serum PTX3 is associated with pulmonary fungal infections.

    • Synonyms

      TSG-14, TNFAIP5, PTX3, Pentraxin-related protein PTX3, Pentaxin-related protein PTX3, Tumor necrosis factor-inducible gene 14 protein, TSG14, pentraxin-related gene rapidly induced by IL-1 beta.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMENS DDYDLMYVNL DNEIDNGLHP TEDPTPCDCG QEHSEWDKLF IMLENSQMRE RMLLQATDDV LRGELQRLRE ELGRLAESLA RPCAPGAPAE ARLTSALDEL LQATRDAGRR LARMEGAEAQ RPEEAGRALA AVLEELRQTR ADLHAVQGWA ARSWLPAGCE TAILFPMRSK KIFGSVHPVR PMRLESFSAC IWVKATDVLN KTILFSYGTK RNPYEIQLYL SYQSIVFVVG GEENKLVAEA MVSLGRWTHL CGTWNSEEGL TSLWVNGELA ATTVEMATGH IVPEGGILQI GQEKNGCCVG GGFDETLAFS GRLTGFNIWD SVLSNEEIRE TGGAESCHIR GNIVGWGVTE IQPHGGAQYV S.

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    Ptx3 Human
  • View Data Sheet

    Name :

    ZNF514 Human

    Description:

    Zinc Finger Protein 514 Human Recombinant

    Zinc finger protein 514, ZNF514.

    Product # :

    PRO-1594

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    Description

    ZNF514 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 423 amino acids (1-400 a.a) and having a molecular mass of 48.3kDa.ZNF514 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ZNF514 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

      Zinc finger protein 514 (ZNF514) is a member of the krueppel C2H2-type zinc-finger proteinfamily. ZNF514 contains 7 C2H2-type zinc fingers and contains 1 KRAB domain. In addition, ZNF514 may be implicated intranscriptional regulation.

    • Synonyms

      Zinc finger protein 514, ZNF514.

    • 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 MGSMTFEDVA VEFSQWEWGQ LNPAQKDLYR EVMLENFRNL AILGLLVSKP YVICQLEEGG EPFMVEREIS TGAHSDWKRR SKSKESMPSW GISKEELFQV VSVEKHIQDV LQFSKLKAAC GCDGQLEMQQ IKQERHLKQM STIHKSATTL SRDYKWNGFG RSLGLRSVLV NQHSILMGEG SYKCDTEFRQ TLGGNNSQRT HPEKKSCKCN ECGKSFHFQS ELRRHQRCHT GEKPYECSDC GRAFGHISSL IKHQRTHTGE KPYECSECGR AFSQSSSLVL HYRFHTGEKP YKCNECGRAF GHTSSLIKHQ RTHTGEKPYE CRECGRTFSQ SSSLIVHYRF HTGEKPYKCN KCGRAFSQSS SLTQHYRFHT GEKPYKCNEC GRAFAHTASL IKHQRSHAGK KTL

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    Znf514 Human
  • View Data Sheet

    Name :

    CFD Human

    Description:

    Complement Factor D Human

    Complement factor D, Adipsin, C3 convertase activator, Properdin factor D, CFD, DF, PFD.

    Product # :

    PRO-2699

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    Description

    Human Complement Factor D produced in Human plasma is glycosylated polypeptide chain having a total molecular mass of 24kDa.

    Source

    Human Plasma.

    Formulation

    CFD protein solution contains 10mM Sodium phosphate and 145mM NaCl, pH 7.3.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CFD is an important component of the alternative pathway of complement activation. CFD cleaves and activates factor B when it binds C3b or a C3b-like protein such as C3 or CVF. CFD is a serine protease that exists as a mature protease, but it exhibits a highly restricted specificity and it appears to be substrate activated. CFD cleaves factor B bound to C3b leading to the release of the Ba fragment and leaving the Bb fragment bound to C3b. The C3b,Bb complex is called a C3 or C5 convertase because it converts these proteins to their active forms by cleaving off the small peptides C3a and C5a, respectively.

    • Synonyms

      Complement factor D, Adipsin, C3 convertase activator, Properdin factor D, CFD, DF, PFD.

    • Physical Appearance

      Sterile filtered solution.

    • Stability

      CFD 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 and HBSAG.

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    Cfd Human
  • View Data Sheet

    Name :

    ANKRD54 Human

    Description:

    Ankyrin Repeat Domain 54 Protein Human Recombinant

    LIAR, Lyn-interacting ankyrin repeat protein.

    Product # :

    PRO-1480

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    Description

    ANKRD54 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 323 amino acids (1-300 a.a.) and having a molecular mass of 34.9kDa.ANKRD54 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ANKRD54 protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer, (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Ankyrin Repeat Domain 54 (ANKRD54), which is also known as LIAR contains 4 ANK repeats. ANKRD54 plays a vital role in regulating intracellular signaling events related with erythroid terminal differentiation. ANKRD54 interacts with LYN through ankyrin repeat region and the SH3-domain in an activation-independent status of LYN. ANKRD54 creates a multiprotein complex with LYN and HCLS1.

    • Synonyms

      LIAR, Lyn-interacting ankyrin repeat protein.

    • 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 MGSMAAAAGD ADDEPRSGHS SSEGECAVAP EPLTDAEGLF SFADFGSALG GGGAGLSGRA SGGAQSPLRY LHVLWQQDAE PRDELRCKIP AGRLRRAARP HRRLGPTGKE VHALKRLRDS ANANDVETVQ QLLEDGADPC AADDKGRTAL HFASCNGNDQ IVQLLLDHGA DPNQRDGLGN TPLHLAACTN HVPVITTLLR GGARVDALDR AGRTPLHLAK SKLNILQEGH AQCLEAVRLE VKQIIHMLRE YLERLGQHEQ RERLDDLCTR LQMTSTKEQV DEVTDLLASF TSLSLQMQSM EKR.

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    Ankrd54 Human
  • View Data Sheet

    Name :

    DGCR6L Human

    Description:

    DiGeorge Syndrome Critical Region Gene 6-Like Human Recombinant

    Protein DGCR6L, DiGeorge syndrome critical region 6-like protein, DGCR6L.

    Product # :

    PRO-1454

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    Description

    DGCR6L Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 243 amino acids (1-220 a.a) and having a molecular mass of 27.3kDa.DGCR6L is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    DGCR6L protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol, 1mM DTT and 250mM Imidazole.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      DiGeorge syndrome critical region 6-like protein (DGCR6L) shares homology with the Drosophila gonadal protein, it is expressed in gonadal tissues and germ cells, and with the human laminin gamma-1 chain which functions in cell attachment and migration. DGCR6L is located in a region of chromosome 22 involved in the DiGeorge syndrome, one aspect of a wider collection of anomalies referred to as the CATCH 22 syndrome. Moreover, it is one of two functional genes encoding nearly identical proteins which have analogous expression patterns.

    • Synonyms

      Protein DGCR6L, DiGeorge syndrome critical region 6-like protein, DGCR6L.

    • 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 MGSMERYAAA LEEVADGARQ QERHYQLLSA LQSLVKELPS SFQQRLSYTT LSDLALALLD GTVFEIVQGL LEIQHLTEKS LYNQRLRLQN EHRVLRQALR QKHQEAQQAC RPHNLPVVQA AQQRELEAVE HRIREEQRAM DQKIILELDR KVADQQSTLE KAGVAGFYVT TNPQELMLQM NLLELIRKLQ QRGCRAGNAA LGLGGPWQSP AAQCDQKGSP VPP.

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    Dgcr6L Human
  • View Data Sheet

    Name :

    FLRT3 Human, HEK

    Description:

    Fibronectin Leucine Rich Transmembrane Protein 3 Human Recombinant, HEK

    Fibronectin Leucine Rich Transmembrane Protein 3, Fibronectin-Like Domain, Containing Leucine-Rich Transmembrane Protein 3, HH21, Leucine-Rich Repeat, Transmembrane Protein FLRT3, KIAA1469.

    Product # :

    PRO-2805

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    Description

    FLRT3 Human Recombinant is a single, glycosylated, polypeptide chain (29-528 a.a) containing a total of 506 amino acids and having a molecular mass of 57.3 kDa. FLRT3 is fused to a 6 a.a his-Tag at C-terminus and is purified by proprietary chromatographic techniques.

    Source

    HEK293 Cells.

    Formulation

    FLRT3 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    >40%.  Measured by the ability of the immobilized protein to support the adhesion of Neuro-2a neuroblast cells. When cells are added to human FLRT3 coated plates 5 ug/ml.

    More Info

    • Synonyms

      Fibronectin Leucine Rich Transmembrane Protein 3, Fibronectin-Like Domain, Containing Leucine-Rich Transmembrane Protein 3, HH21, Leucine-Rich Repeat, Transmembrane Protein FLRT3, KIAA1469.

    • 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

      KSCPSVCRCD AGFIYCNDRF LTSIPTGIPE DATTLYLQNN QINNAGIPSD LKNLLKVERI YLYHNSLDEF PTNLPKYVKE LHLQENNIRT ITYDSLSKIP YLEELHLDDN SVSAVSIEEG AFRDSNYLRL LFLSRNHLST IPWGLPRTIE ELRLDDNRIS TISSPSLQGL TSLKRLVLDG NLLNNHGLGD KVFFNLVNLT ELSLVRNSLT AAPVNLPGTN LRKLYLQDNH INRVPPNAFS
      YLRQLYRLDM SNNNLSNLPQ GIFDDLDNIT QLILRNNPWY CGCKMKWVRD WLQSLPVKVN VRGLMCQAPE KVRGMAIKDL NAELFDCKDS GIVSTIQITT AIPNTVYPAQ GQWPAPVTKQ PDIKNPKLTK DHQTTGSPSR KTITITVKSV TSDTIHISWK LALPMTALRL SWLKLGHSPA FGSITETIVT GERSEYLVTA LEPDSPYKVC MVPMETSNLY LFDETPVCIE TETAPLRMYN
      PTTTLNREQE KEPYKNPNLP HHHHHH.

    • Background

      Fibronectin leucine-rich transmembrane protein 3, commonly known as FLRT3, stands as a molecular architect in the intricate landscape of neural development. Its roles, initially discovered in the embryonic nervous system, have expanded to encompass various physiological and pathological processes in both the brain and beyond. This research endeavors to unravel the enigma of FLRT3 protein, exploring its structural intricacies, physiological functions, and its far-reaching implications in neurobiology, embryogenesis, and disease. By delving into FLRT3's multifaceted roles, scientists aim to decipher the underlying mechanisms that govern its diverse functions and explore potential therapeutic avenues in the realms of neuroscience and beyond.

      Structural Complexities of FLRT3:

      FLRT3 belongs to the FLRT family, characterized by extracellular leucine-rich repeats (LRRs) and a transmembrane domain. These structural motifs enable FLRT3 to participate in a myriad of interactions, including binding with cell adhesion molecules and guidance cues. Understanding the three-dimensional architecture of FLRT3 is fundamental for unraveling its molecular partnerships, biological activities, and its contributions to cell adhesion and signaling.

      Physiological Functions in Neural Development:

      In the developing nervous system, FLRT3 acts as a guidance molecule, steering growing axons and dendrites to their precise destinations. Through interactions with other cell surface receptors and ligands, FLRT3 modulates axon pathfinding, synapse formation, and neuronal migration. Its presence in growth cones and developing neural circuits underscores its significance in sculpting the intricate neural networks essential for proper brain function.

      Beyond Neural Development:

      Beyond its canonical roles in neurodevelopment, FLRT3 has emerged as a versatile player in various physiological processes. It participates in tissue morphogenesis, modulates cell adhesion, and influences immune responses. Recent studies have also implicated FLRT3 in cancer progression, highlighting its involvement in pathological conditions and making it a potential target for therapeutic interventions in cancer therapy.

      FLRT3 as a Therapeutic Target:

      The diverse roles of FLRT3 in neural development and diseases position it as an attractive target for therapeutic interventions. Modulating FLRT3 interactions offers novel avenues for neurological disorder treatments, including neurodevelopmental disorders and neurodegenerative diseases. Moreover, understanding FLRT3's involvement in cancer biology opens doors for innovative cancer therapies, making it a promising target for precision medicine approaches.

      FLRT3, with its intricate structural features and diverse functional roles, stands as a linchpin in the realms of neuroscience, embryogenesis, and disease. Its multifaceted contributions to neural development, tissue morphogenesis, and disease pathogenesis underscore its significance in both health and pathology. As researchers continue to unravel FLRT3’s complexities, they not only deepen our understanding of fundamental biological processes but also pave the way for groundbreaking discoveries in neuroscience and therapeutic interventions, ultimately shaping the future landscape of medicine and scientific inquiry.

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    Flrt3 Protein
  • View Data Sheet

    Name :

    MAP2K1 Human

    Description:

    Mitogen-Activated Protein Kinase Kinase 1 Human Recombinant

    MAP2K1, MEK1, PRKMK1, MKK1, MAPKK 1, MAP kinase kinase 1.

    Product # :

    PKA-112

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    Description

    MAP2K1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 402 amino acids (1-393a.a.) and having a molecular mass of 44.5kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).MAP2K1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    MAP2K1 protein solution (0.25mg/ml) contains 10% glycerol & Phosphate Buffered Saline (pH 7.4).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      The MAP2K1 protein is encoded by the MAP2K1 gene. This enzyme serves as a MAP (mitogen activated protein) kinase, it is a part of the dual specificity protein kinase family. Extracellular signal-regulated kinases such as MAP kinases has an important role in assimilation of various biochemical signals. MAP2K1 is located upstream to the MAP kinases and activates them by multiple intra and extracellular signals. The enzyme serves as a key factor in the signal transduction pathway of MAP kinase, therefore it takes part in the cell development (transcription regulation, proliferation, differentiation etc.).

    • Synonyms

      MAP2K1, MEK1, PRKMK1, MKK1, MAPKK 1, MAP kinase kinase 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

      ADPMPKKKPT PIQLNPAPDG SAVNGTSSAE TNLEALQKKL EELELDEQQR KRLEAFLTQK QKVGELKDDD FEKISELGAG NGGVVFKVSH KPSGLVMARK LIHLEIKPAI RNQIIRELQV LHECNSPYIV GFYGAFYSDG EISICMEHMD GGSLDQVLKK AGRIPEQILG KVSIAVIKGL TYLREKHKIM HRDVKPSNIL VNSRGEIKLC DFGVSGQLID SMANSFVGTR SYMSPERLQG THYSVQSDIW SMGLSLVEMA VGRYPIPPPD AKELELMFGC QVEGDAAETP PRPRTPGRPL SSYGMDSRPP MAIFELLDYI VNEPPPKLPS GVFSLEFQDF VNKCLIKNPA ERADLKQLMV HAFIKRSDAE EVDFAGWLCS TIGLNQPSTP THAAGVHHHH HH.

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    Map2K1 Human
  • View Data Sheet

    Name :

    AMTN Human

    Description:

    Amelotin Human Recombinant

    UNQ689, Amelotin, PRO1329.

    Product # :

    PRO-1301

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    Description

    AMTN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 216 amino acids (17-209 a.a.) and having a molecular mass of 22.2kDa.AMTN is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    AMTN protein solution (0.5mg/ml) contains mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 20% glycerol and 2mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      AMTN is a member of the amelotin family. AMTN is a lately discovered secreted enamel protein. AMTN mainly expressed during the maturation stage of enamel formation. AMTN gathers in a basal lamina-like structure at the interface between ameloblasts and enamel mineral and it co-localizes with one more lately described enamel protein, odontogenic ameloblast- related protein (ODAM(.

    • Synonyms

      UNQ689, Amelotin, PRO1329.

    • 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 MGSLPQLKPA LGLPPTKLAP DQGTLPNQQQ SNQVFPSLSL IPLTQMLTLG PDLHLLNPAA GMTPGTQTHP LTLGGLNVQQ QLHPHVLPIF VTQLGAQGTI LSSEELPQIF TSLIIHSLFP GGILPTSQAG ANPDVQDGSL PAGGAGVNPA TQGTPAGRLP TPSGTDDDFA VTTPAGIQRS THAIEEATTE SANGIQ.

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    Amtn Human
  • View Data Sheet

    Name :

    CCL24 Mouse

    Description:

    Eotaxin-2 Mouse Recombinant (CCL24)

    C-C motif chemokine 24, Small-inducible cytokine A24, Myeloid progenitor inhibitory factor 2, CK-beta-6, Eosinophil chemotactic protein 2, Eotaxin-2, CCL24, Ckb-6, MPIF2, MPIF-2, SCYA24, Eotaxin2, CCL-24.

    Product # :

    CHM-368

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    Description

    CCL24 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 93 amino acids and having a molecular mass of 10.3 kDa. The CCL24 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CCL24 protein was lyophilized from a concentrated (1mg/ml) sterile solution containing 20mM Phosphate buffer pH-7.4 and 0.15M sodium chloride.

    Purity

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

    Biological Activity

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

    More Info

    • Introduction

      Eotaxin-2, also called MPIF2 & Ckb6, is a novel CC chemokine produced by activated monocytes and T lymphocytes. Eotaxin-2 selectively chemoattracts cells expressing CCR3 including eosinophils, basophils, Th2 T cells, mast cells, and certain subsets of dendritic cells. Furthermore, Eotaxin-2 inhibits the proliferation of multipotential hematopoietic progenitor cells. The mature protein, which includes C-terminal truncation, contains 78 amino acids (92 amino acids for the mouse homolog, without C-terminal truncation).
      CCL24 functions as a chemotactic chemokine for resting t-lymphocytes, and eosinophils. CCL24 has lower chemotactic activity for neutrophils but none for monocytes and activated lymphocytes. CCL24 is a strong suppressor of colony formation by a multipotential hematopoietic progenitor cell line and binds to CCR3.

    • Synonyms

      C-C motif chemokine 24, Small-inducible cytokine A24, Myeloid progenitor inhibitory factor 2, CK-beta-6, Eosinophil chemotactic protein 2, Eotaxin-2, CCL24, Ckb-6, MPIF2, MPIF-2, SCYA24, Eotaxin2, CCL-24.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Eotaxin-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL24 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 CCL24 Mouse Recombinant in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      VTIPSSCCTS FISKKIPENR VVSYQLANGS ICPKAGVIFI TKKGHKICTD PKLLWVQRHI QKLDAKKNQP SKGAKAVRTK FAVQRRRGNS TEV.

    • Background

      What is the molecular weight/Mw of CCL24 MOUSE Protein?
      CCL24 MOUSE Protein has a total Mw of 10.3kDa.

      What is the source or expression system of CCL24 MOUSE Protein?
      Escherichia Coli.

      What is the Purity of CCL24 MOUSE Protein?
      CCL24 MOUSE Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCL24 MOUSE Protein?
      Determined by its ability to chemoattract murine lymphocytes using a concentration range of 10-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.

      What is the amino acid sequence of CCL24 MOUSE Protein?
      VTIPSSCCTS FISKKIPENR VVSYQLANGS ICPKAGVIFI TKKGHKICTD PKLLWVQRHI QKLDAKKNQP SKGAKAVRTK FAVQRRRGNS TEV.

      What applications can CCL24 MOUSE Protein be used in?
      CCL24 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CCL24 MOUSE Protein?
      The endotoxin level is minimal, CCL24 MOUSE 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.

    Ccl24 Mouse
  • View Data Sheet

    Name :

    CGB Human

    Description:

    CGB Human Recombinant

    CGB3, CGB5, CGB7, CGB8, hCGB,  CG-beta, CGB.

    Product # :

    HOR-007

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    CGB Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 168 amino acids (21-165 a.a.) and having a molecular mass of 17.9kDa. CGB is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CGB protein solution (0.5mg/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

      Glycoprotein hormones are heterodimers consisting of a common alpha subunit and a unique beta subunit which confers biological specificity. CGB is a member of the glycoprotein hormone beta chain family and is the beta 3 subunit of (CG). CG is produced by the trophoblastic cells of the placenta and stimulates the ovaries. The beta subunit of CG is encoded by 6 genes which are arranged in tandem and inverted pairs on chromosome 19q13.3 and contiguous with the luteinizing hormone beta subunit gene.

    • Synonyms

      CGB3, CGB5, CGB7, CGB8, hCGB, CG-beta, CGB.

    • 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 MGSSKEPLRP RCRPINATLA VEKEGCPVCI TVNTTICAGY CPTMTRVLQG VLPALPQVVC NYRDVRFESI RLPGCPRGVN PVVSYAVALS CQCALCRRST TDCGGPKDHP LTCDDPRFQD SSSSKAPPPS LPSPSRLPGP SDTPILPQ.

    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.

    Cgb Human
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