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Search results

1000 results found for “Centromere Protein”

Name

Description

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  • View Data Sheet

    Name :

    ADAM10 Human

    Description:

    A Disintegrin and Metalloproteinase Domain 10 Human Recombinant

    Kuz, AD10, MADM, CD156c, HsT18717, ADAM metallopeptidase domain 10, A disintegrin and metalloproteinase domain 10, Mammalian disintegrin-metalloprotease, Kuzbanian protein homolog, CDw156, ADAM 10, ADAM10.

    Product # :

    PRO-476

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    Description

    ADAM10 extracellular domain minus the signal peptide and pro-sequence Human Recombinant fused to N-terminal His-Tag produced in E.Coli is a single, non-glycosylated polypeptide chain containing 459 amino acids (214-672) and having a molecular mass of 55.089kDa.

    Source

    Escherichia Coli.

    Formulation

    The ADAM10 solution contains 20mM Tris (pH 8), 1mM EDTA and 50% Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      ADAM10 is part of the ADAM family which are cell surface proteins with a distinctive structure possessing both potential adhesion and protease domains. ADAM10 cleaves many proteins including TNF-alpha and E-cadherin. ADAM10 cleaves the membrane-bound precursor of tnf-alpha at 76- ala-|-val-77 to its mature soluble form. ADAM10 is in charge for the proteolytic release of several other cell-surface proteins, including ephrin-a2 and for constitutive and regulated alpha-secretase cleavage of amyloid precursor protein. ADAM10 is involved in the normal cleavage of the cellular prion protein. ADAM10 is involved in the cleavage of the adhesion molecule l1 at the cell surface and in the release of membrane vesicles, suggesting a vesicle-based protease activity. ADAM10 controls the proteolytic processing of notch and mediates lateral inhibition during neurogenesis.

    • Synonyms

      Kuz, AD10, MADM, CD156c, HsT18717, ADAM metallopeptidase domain 10, A disintegrin and metalloproteinase domain 10, Mammalian disintegrin-metalloprotease, Kuzbanian protein homolog, CDw156, ADAM 10, ADAM10.

    • 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.

    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.

    Adam10 Human
  • View Data Sheet

    Name :

    SNCA NACP112 Human

    Description:

    Alpha Synuclein NACP112 Human Recombinant

    Alpha-synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, NACP, PD1, PARK1, PARK4, MGC110988, a-Synuclein, SNCA.

    Product # :

    PRO-162

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    Description

    A-Synuclein NACP112 Human Recombinant which is an alternatively spliced (103-129) form of a-Synuclein, produced in E.Coli is a single, non-glycosylated polypeptide chain of 112 amino acids having a molecular mass of 11.3kDa. The Recombinant Human a-Synuclein NACP112 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SNCA NACP112 protein solution (1mg/ml) contains 20mM Tris-HCl buffer pH 7.5 and 100mM NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      a-Synuclein (amino acids 1-140), an acidic neuronal protein of 140 amino acids, is extremely heat-resistant and is natively unfolded with an extended structure primarily composed of random coils. a-synuclein has been suggested to be implicated in the pathogenesis of Parkinson’s disease and related neurodegenerative disorders, and more recently, to be an important regulatory component of vesicular transport in neuronal cells. Moreover, recent studies have shown that a-synuclein has chaperone activity and that this activity is lost upon removing its C-terminal acidic tail (amino acids 96-140).

    • Synonyms

      Alpha-synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, NACP, PD1, PARK1, PARK4, MGC110988, a-Synuclein, SNCA.

    • 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

      MDVFMKGLSK AKEGVVAAAE KTKQGVAEAA GKTKEGVLYV GSKTKEGVVH GVATVAEKTK EQVTNVGGAV VTGVTAVAQK TVEGAGSIAA ATGFVKKDQL GKEGYQDYEP EA.

    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.

    Snca Nacp112 Human
  • View Data Sheet

    Name :

    THOC7 Human

    Description:

    THO Complex 7 Human Recombinant

    THO Complex 7, Functional Spliceosome-Associated Protein 24, NIF3L1BP1, Ngg1-Interacting Factor 3-Like Protein 1-Binding Protein 1, Ngg1 Interacting Factor 3 Like 1 Binding Protein 1, NIF3L1-Binding Protein 1, HTREX30, FSAP24, THO Complex 7 Homolog (Drosophila), THO Complex Subunit 7 Homolog, THO Complex 7 Homolog, fSAP24, hTREX30.

    Product # :

    PRO-2163

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    Description

    THOC7 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 227 amino acids (1-204 a.a) and having a molecular mass of 26.1kDa.THOC7 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    THOC7 protein solution (0. 5mg/ml) containing Phosphate buffered saline (pH7.4) and 50% glycerol, 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      THO Complex 7, also known as THOC7, is a component of the THO subcomplex of the TREX complex which couples mRNA transcription, processing and nuclear export, and which related to spliced mRNA. THOC7 is a protein coding gene which is essential for export of polyadenylated RNA. Furthermore, THOC7 is associated with RNA transport.

    • Synonyms

      THO Complex 7, Functional Spliceosome-Associated Protein 24, NIF3L1BP1, Ngg1-Interacting Factor 3-Like Protein 1-Binding Protein 1, Ngg1 Interacting Factor 3 Like 1 Binding Protein 1, NIF3L1-Binding Protein 1, HTREX30, FSAP24, THO Complex 7 Homolog (Drosophila), THO Complex Subunit 7 Homolog, THO Complex 7 Homolog, fSAP24, hTREX30.

    • 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 MGSMGAVTDD EVIRKRLLID GDGAGDDRRI NLLVKSFIKW CNSGSQEEGY SQYQRMLSTL SQCEFSMGKT LLVYDMNLRE MENYEKIYKE IECSIAGAHE KIAECKKQIL QAKRIRKNRQ EYDALAKVIQ HHPDRHETLK ELEALGKELE HLSHIKESVE DKLELRRKQF HVLLSTIHEL QQTLENDEKL SEVEEAQEAS METDPKP.

    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.

    Thoc7 Human
  • View Data Sheet

    Name :

    CRK Human

    Description:

    V-crk Sarcoma Virus CT10 Oncogene Human Recombinant

    Adapter molecule crk, Proto-oncogene c-Crk, p38, CRK, CRKII.

    Product # :

    PRO-275

    Price :

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    Description

    CRK Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 224 amino acids (1-204 a.a.) and having a molecular mass of 25kDa. The CRK is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CRK solution (0.5 mg/ml) contains 20mM Tris-HCl Buffer (pH 8.0) and 10% Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CRK belongs to the signaling adapter protein family which binds to several tyrosine-phosphorylated proteins. CRK is involved in many cellular processes such as apoptosis, proliferation, and differentiation. CRK has a modular domain architecture consisting of an SH2 followed by two SH3 domains (src-homology domains). The N-terminal SH2 domain of the CRK protein functions as a positive regulator of transformation whereas the C-terminal SH3 domain functions as a negative regulator of transformation.

    • Synonyms

      Adapter molecule crk, Proto-oncogene c-Crk, p38, CRK, CRKII.

    • 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).Please prevent freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MAGNFDSEER SSWYWGRLSR QEAVALLQGQ RHGVFLVRDS STSPGDYVLS VSENSRVSHY IINSSGPRPP VPPSPAQPPP GVSPSRLRIG DQEFDSLPAL LEFYKIHYLD TTTLIEPVSR SRQGSGVILR QEEAEYVRAL FDFNGNDEED LPFKKGDILR IRDKPEEQWW NAEDSEGKRG MIPVPYVEKY RPASASVSAL IGGR.

    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.

    CRK Human
  • View Data Sheet

    Name :

    NME4 Human

    Description:

    Non-Metastatic Cells 4 Human Recombinant

    Non-metastatic cells 4, nm23-H4, NM23H4, Nucleoside diphosphate kinase D, NDK, NDPKD, NDP kinase mitochondrial, EC 2.7.4.6, NDPK-D.

    Product # :

    PRO-219

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    Description

    NME4 Human Recombinant fused with a 21 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 176 amino acids (33-187a.a.) and having a molecular mass of 19.6kDa. The NME4 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The NME4 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 40% glycerol and 0.2M NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      NME4 is a member of the NDK family. NME4 are ubiquitous enzymes which catalyze transfer of gamma-phosphates, using a phosphohistidine intermediate, between nucleoside and dioxynucleoside tri- and diphosphates. The enzymes are products of the nm23 gene family that include NME4. NME4 has a key part in the synthesis of nucleoside triphosphates other than ATP.

    • Synonyms

      Non-metastatic cells 4, nm23-H4, NM23H4, Nucleoside diphosphate kinase D, NDK, NDPKD, NDP kinase mitochondrial, EC 2.7.4.6, NDPK-D.

    • 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 MPSWTRERTL VAVKPDGVQR RLVGDVIQRF ERRGFTLVGM KMLQAPESVL AEHYQDLRRK PFYPALIRYM SSGPVVAMVW EGYNVVRASR AMIGHTDSAE AAPGTIRGDF SVHISRNVIH ASDSVEGAQR EIQLWFQSSE LVSWADGGQH SSIHPA.

    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.

    Nme4 Human
  • View Data Sheet

    Name :

    PDRG1 Human

    Description:

    p53 and DNA-Damage Regulated 1 Human Recombinant

    p53 and DNA damage-regulated protein 1, PDRG1, C20orf126, PDRG.

    Product # :

    PRO-007

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    Description

    PDRG1 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 153 amino acids (1-133 a.a.) and having a molecular mass of 17.6kDa. The PDRG1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PDRG1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 5mM DTT and 20% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      PDRG1 is a 133 amino acid protein that localizes to the cytoplasm and belongs to the prefoldin subunit beta family. PDRG1 is expressed primarily in normal testicular tissue, it is functionally induced by ultraviolet light and is thought to have a role in chaperone-mediated protein folding, possibly having a role in cellular degradation. PDRG1 is linked to Creutzfeldt-Jakob disease, amyotrophic lateral sclerosis, spinal muscular atrophy, ring chromosome 20 epilepsy syndrome and Alagille syndrome.

    • Synonyms

      p53 and DNA damage-regulated protein 1, PDRG1, C20orf126, PDRG.

    • 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 MLSPEAERVL RYLVEVEELA EEVLADKRQI VDLDTKRNQN REGLRALQKD LSLSEDVMVC FGNMFIKMPH PETKEMIEKD QDHLDKEIEK LRKQLKVKVN RLFEAQGKPE LKGFNLNPLN QDELKALKVI LKG.

    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.

    Pdrg1 Human
  • View Data Sheet

    Name :

    RBM17 Human

    Description:

    RNA Binding Motif Protein 17 Human Recombinant

    RNA Binding Motif Protein 17, SPF45, Splicing Factor 45kDa, RNA-Binding Motif Protein 17, Splicing Factor 45, 45 kDa-splicing factor, RBM17.

    Product # :

    PRO-1793

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    Description

    RBM17 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 421 amino acids (1-401 a.a) and having a molecular mass of 47.1kDa.RBM17 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    RBM17 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      RNA binding motif protein 17 (RBM17) is a splice factor which binds to the single stranded 3'AG at the exon/intron border and promotes its utilization in the 2nd catalytic step. The RBM17 protein is involved in the regulation of alternative splicing and the utilization of cryptic splice sites. RBM17 protein also stimulates the utilization of a cryptic splice site created by the beta-110 mutation in the HBB gene. The ensuing frameshift leads to sickle cell anemia.

    • Synonyms

      RNA Binding Motif Protein 17, SPF45, Splicing Factor 45kDa, RNA-Binding Motif Protein 17, Splicing Factor 45, 45 kDa-splicing factor, RBM17.

    • 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 MSLYDDLGVE TSDSKTEGWS KNFKLLQSQL QVKKAALTQA KSQRTKQSTV LAPVIDLKRG GSSDDRQIVD TPPHVAAGLK DPVPSGFSAG EVLIPLADEY DPMFPNDYEK VVKRQREERQ RQRELERQKE IEEREKRRKD RHEASGFARR PDPDSDEDED YERERRKRSM GGAAIAPPTS LVEKDKELPR DFPYEEDSRP RSQSSKAAIP PPVYEEQDRP RSPTGPSNSF LANMGGTVAH KIMQKYGFRE GQGLGKHEQG LSTALSVEKT SKRGGKIIVG DATEKDASKK SDSNPLTEIL KCPTKVVLLR NMVGAGEVDE DLEVETKEEC EKYGKVGKCV IFEIPGAPDD EAVRIFLEFE RVESAIKAVV DLNGRYFGGR VVKACFYNLD KFRVLDLAEQ V.

    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.

    Rbm17 Human
  • View Data Sheet

    Name :

    STMN3 Human

    Description:

    Stathmin Like-3 Human Recombinant

    Stathmin-3, SCG10-like protein, STMN3, SCLIP

    Product # :

    PRO-838

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    Description

    STMN3 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 163 amino acids (39-180 a.a.) and having a molecular mass of 18.9 kDa. The STMN3 is fused to a 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    STMN3 Human solution containing 20mM Tris-HCl pH-8, 1mM DTT & 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      STMN3 is a neuronal specific protein which belongs to the stathmin/oncoprotein 18 family of microtubule-destabilizing phosphoproteins. It is similar to the SCG10 protein and is involved in signal transduction and regulation of microtubule dynamics.

    • Synonyms

      Stathmin-3, SCG10-like protein, STMN3, SCLIP

    • 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 MDMEVKQLDK RASGQSFEVI LKSPSDLSPE SPMLSSPPKK KDTSLEELQK RLEAAEERRK TQEAQVLKQL AERREHEREV LHKALEENNN FSRQAEEKLN YKMELSKEIR EAHLAALRER LREKELHAAE VRRNKEQREE MSG.

    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.

    Stmn3 Human
  • View Data Sheet

    Name :

    SUMO2 Human

    Description:

    Small Ubiquitin-Related Modifier 2 Human Recombinant

    Small ubiquitin-related modifier 2, SUMO-2, Ubiquitin-like protein SMT3B, SMT3 homolog 2, Sentrin-2, HSMT3, SUMO-3, SUMO2, SMT3B, SMT3H2, MGC117191.

    Product # :

    PRO-586

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    Description

    SUMO2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 93 amino acids and having a molecular mass of 10.6 kDa.The SUMO-2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SUMO2 (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Small Ubiquitin-like Modifiers (SUMOs) are a family of small, related proteins that can be enzymatically attached to a target protein by a post-translational modification process termed sumoylation. Unlike ubiquitination, which targets proteins for degradation, sumoylation participates in a number of cellular processes, such as nuclear transport, transcriptional regulation, apoptosis, and protein stability. All SUMO proteins share the conserved ubiquitin domain and the C-terminal diglycine cleavage/attachment site. Human SUMO2, also known as Sentrin2 and SMT3B is synthesized as a 95 amino acid (aa), 11 kDa propeptide that contains a two aa C-terminal prosegment, and an 18 aa N-terminal protein interacting region (aa 33 -50). Following prosegment cleavage, the C-terminal glycine is enzymatically attached to a lysine on a target protein. Human SUMO2 shares 100% sequence identity to SUMO-2 from mouse. SUMO2 also has very high sequence homology to SUMO3 and SUMO4, 86 % and 85%, respectively. SUMO2 shares only 44% sequence identity to SUMO1.

    • Synonyms

      Small ubiquitin-related modifier 2, SUMO-2, Ubiquitin-like protein SMT3B, SMT3 homolog 2, Sentrin-2, HSMT3, SUMO-3, SUMO2, SMT3B, SMT3H2, MGC117191.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Can be stored at +4C for 1 week. For long term storage , below -20C.Please prevent freeze-thaw cycles.

    • Amino Acid Sequence

      MADEKPKEGVKTENNDHINLKVAGQDGSVVQFKIKRHTPLSKLMKAYC
      ERQGLSMRQIRFRFDGQPINETDTPAQLEMEDEDTIDVFQQQTGG.

    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.

    Sumo2 Human
  • View Data Sheet

    Name :

    HNRNPA1 Human

    Description:

    Heterogeneous Nuclear Ribonucleoprotein A1 Human Recombinant

    Heterogeneous nuclear ribonucleoprotein A1, hnRNP A1, Helix-destabilizing protein, Single-strand RNA-binding protein, hnRNP core protein A1, HNRNPA1, HNRPA1, HNRPA1L3, hnRNP-A1.

    Product # :

    PRO-1038

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    Description

    HNRNPA1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 343 amino acids (1-320 a.a.) and having a molecular mass of 36.6kDa.HNRNPA1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    HNRNPA1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 40% glycerol, 0.15M NaCl and 1mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Heterogeneous nuclear ribonucleoprotein A1 (HNRNPA1) is a member of the A/B subfamily of ubiquitously expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). HNRNPA1 is involved in the packing of pre-mRNA into hnRNP particles, transport of poly(A) mRNA from the nucleus to the cytoplasm and may control splice site selection. The HNRNPA1 protein may also have a role in HCV RNA replication. In addition, HNRNPA1 is believed to have a key role in the formation of specific myometrial protein species in parturition.
      The hnRNP proteins have distinctive nucleic acid binding properties. HNRNPA1 has 2 repeats of quasi-RRM domains that bind to RNAs. HNRNPA1 is one of the most copious core proteins of hnRNP complexes and it is restricted to the nucleoplasm. The HNRNPA1 protein, along with other hnRNP proteins, is exported from the nucleus, most likely bound to mRNA, and is immediately re-imported. The M9 domain of HNRNPA1 functions as both a nuclear localization and nuclear export signal.

    • Synonyms

      Heterogeneous nuclear ribonucleoprotein A1, hnRNP A1, Helix-destabilizing protein, Single-strand RNA-binding protein, hnRNP core protein A1, HNRNPA1, HNRPA1, HNRPA1L3, hnRNP-A1.

    • 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 MGSMSKSESP KEPEQLRKLF IGGLSFETTD ESLRSHFEQW GTLTDCVVMR DPNTKRSRGF GFVTYATVEE VDAAMNARPH KVDGRVVEPK RAVSREDSQR PGAHLTVKKI FVGGIKEDTE EHHLRDYFEQ YGKIEVIEIM TDRGSGKKRG FAFVTFDDHD SVDKIVIQKY HTVNGHNCEV RKALSKQEMA SASSSQRGRS GSGNFGGGRG GGFGGNDNFG RGGNFSGRGG FGGSRGGGGY GGSGDGYNGF GNDGSNFGGG GSYNDFGNYN NQSSNFGPMK GGNFGGRSSG PYGGGGQYFA KPRNQGGYGG SSSSSSYGSG RRF.

    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.

    Hnrnpa1 Human
  • View Data Sheet

    Name :

    PCNA Human

    Description:

    Proliferating Cell Nuclear Antigen Human Recombinant

    Proliferating cell nuclear antigen, PCNA, Cyclin, MGC8367.

    Product # :

    PRO-615

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    Description

    PCNA Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 261 amino acids (1-261 a.a) and having a molecular mass of 28.7kDa. PCNA is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PCNA solution contains 20mM Tris pH-7.5 & 2mM EDTA & 20% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      PCNA is located in the nucleus and is a cofactor of DNA polymerase delta. PCNA acts as a homotrimer and helps elevate the processivity of leading strand synthesis during DNA replication. In reaction to DNA damage, PCNA is ubiquitinated and takes part in the RAD6-dependent DNA repair pathway. 2 transcript variants encoding the same protein have been found for PCNA gene. Pseudogenes of this PCNA gene have been described on chromosome 4 and on the X chromosome. PCNA is expressed during late G1- phase, S-phase of mitosis and persists until the end of the M-phase because of its long biological half-life. PCNA is induced by UV irradiation.

    • Synonyms

      Proliferating cell nuclear antigen, PCNA, Cyclin, MGC8367.

    • 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

      MFEARLVQGS ILKKVLEALK DLINEACWDI SSSGVNLQSM DSSHVSLVQLTLRSEGFDTY RCDRNLAMGV NLTSMSKILK CAGNEDIITL RAEDNADTLA LVFEAPNQEK VSDYEMKLMD LDVEQLGIPE QEYSCVVKMP SGEFARICRD LSHIGDAVVI SCAKDGVKFS ASGELGNGNI KLSQTSNVDK EEEAVTIEMN EPVQLTFALR YLNFFTKATP LSSTVTLSMS ADVPLVVEYK IADMGHLKYY LAPKIEDEEG S.

    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.

    Pcna Human
  • View Data Sheet

    Name :

    SHH Rat

    Description:

    Sonic HedgeHog Rat Recombinant

    SHH, HHG-1, HHG1, Sonic hedgehog protein, TPT, HLP3, HPE3, SMMCI, TPTPS, MCOPCB5.

    Product # :

    CYT-1099

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    Description

    Sonic HedgeHog Recombinant Rat produced in E.Coli is a single, non-glycosylated polypeptide chain containing 176 amino acids and having a molecular mass of 19.9kDa. SHH is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SHH is lyophilized from a sterile (0.2 µm) filtered solution containing 10 mM sodium phosphate, pH 7.5.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Recombinant Human Sonic Hedgehog is part of a small group of secreted proteins that are vital for development in both vertebrates and invertebrates. 3 mammalian hedgehog genes (sonic, desert, Indian) share about 60% homology. The Human Sonic Hedgehog is 99% homologous to the mouse gene. Sonic HedgeHog helps in guiding the early embryo. It has been associated as the major inductive signal in patterning of the ventral neural tube, the anterior-posterior limb axis, and the ventral somites. Sonic HedgeHog binds to the patched receptor, which association with smoothened, to activate the transcription of target genes. In the absence of sonic HedgeHog, patched receptor represses the constitutive signaling activity of smoothened. Sonic HedgeHog also regulates another factor, the gli oncogene. Sonic HedgeHog intercellular signal is necessary for a various patterning events during development: signal produced by the notochord that induces ventral cell fate in the neural tube and somites, and the polarizing signal for patterning of the anterior-posterior axis of the developing limb bud. Sonic HedgeHog exhibits both floor plate- and motor neuron-inducing activity. Mutations in a long-range Sonic HedgeHog enhancer located in an intron of the limb region 1 gene result in preaxial polydactyly.

    • Synonyms

      SHH, HHG-1, HHG1, Sonic hedgehog protein, TPT, HLP3, HPE3, SMMCI, TPTPS, MCOPCB5.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MIIGPGRGFG KRQHPKKLTP LAYKQFIPNV AEKTLGASGR YEGKITRNSE RFKELTPNYN PDIIFKDEEN TGADRLMTQR CKDKLNALAI SVMNQWPGVK LRVTEGWDED GHHSEESLHY EGRAVDITTS DRDRSKYGML ARLAVEAGFD WVYYESKARI HCSVKAENSV AAKSDG.

    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.

    Shh Rat
  • View Data Sheet

    Name :

    Vimentin Human

    Description:

    Vimentin Human Recombinant

    Vimentin, Vim, FLJ36605.

    Product # :

    PRO-309

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    Description

    Vimentin Human Recombinant produced in E.coli cells is a single non-glycosylated protein containing 465 amino acids chain and having a molecular mass of 53.5kDa. The Vimentin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Vimentin 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 RP-HPLC.
    (b) Analysis by SDS-PAGE.

    More Info

    • Introduction

      Vimentin expression in human malignant glioma cells depends on cellular density, algorithms of drug delivery and chemo/radio treatment. Vimentin and detyrosinated microtubules provide structural support for the extensive microtentacles observed in detached tumor cells and a mechanism to promote successful metastatic spread. Primary colorectal carcinomas display aberrant expression of vimentin, and have activated Notch and TGFbeta signaling pathways. Vimentin is a strong arterial substrate for transglutaminases. Transglutaminase-mediated vimentin dimerization results in a novel unifying pathway by which vasodilatory and remodeling responses may be regulated. Ablation of vimentin expression inhibits migration and invasion of colon and breast cancer cell lines. Vimentin is the main intermediate filament protein in mesenchymal cells and is therefore of value in the differential diagnosis of undifferentiated neoplasms.

    • Synonyms

      Vimentin, Vim, FLJ36605.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      STRSVSSSSY RRMFGGPGTA SRPSSSRSYV TTSTRTYSLG SALRPSTSRS LYASSPGGVY ATRSSAVRLR SSVPGVRLLQ DSVDFSLADA INTEFKNTRT NEKVELQELN DRFANYIDKV RFLEQQNKIL LAELEQLKGQ GKSRLGDLYE EEMRELRRQV DQLTNDKARV EVERDNLAED IMRLREKLQE EMLQREEAEN TLQSFRQDVD NASLARLDLE RKVESLQEEI AFLKKLHEEE IQELQAQIQE QHVQIDVDVS KPDLTAALRD VRQQYESVAA KNLQEAEEWY KSKFADLSEA ANRNNDALRQ AKQESTEYRR QVQSLTCEVD ALKGTNESLE RQMREMEENF AVEAANYQDT IGRLQDEIQN MKEEMARHLR EYQDLLNVKM ALDIEIATYR KLLEGEESRI SLPLPNFSSL NLRETNLDSL PLVDTHSKRT LLIKTVETRD GQVINETSQH HDDLE.

    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.

    Vimentin Human
  • View Data Sheet

    Name :

    TFB1M Human

    Description:

    Transcription Factor B1, Mitochondrial Human Recombinant

    Dimethyladenosine transferase 1 mitochondrial, Mitochondrial 12S rRNA dimethylase 1, Mitochondrial transcription factor B1, h-mtTFB, h-mtTFB1, hTFB1M, mtTFB1, S-adenosylmethionine-6-N'-N'-adenosyl(rRNA) dimethyltransferase 1, TFB1M, CGI-75, CGI75, mtTFB.

    Product # :

    PRO-903

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    Description

    TFB1M Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 340 amino acids (28-346 a.a.) and having a molecular mass of 38.8kDa.TFB1M is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TFB1M protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      TFB1M is a member of the methyltransferase superfamily. TFB1M is a dimethyltransferase which methylates mitochondrial 12S rRNA at the conserved stem loop. The TFB1M protein also is part of the basal mitochondrial transcription complex and is required for mitochondrial gene expression. TFB1M stimulates transcription independently of the methyltransferase activity.

    • Synonyms

      Dimethyladenosine transferase 1 mitochondrial, Mitochondrial 12S rRNA dimethylase 1, Mitochondrial transcription factor B1, h-mtTFB, h-mtTFB1, hTFB1M, mtTFB1, S-adenosylmethionine-6-N'-N'-adenosyl(rRNA) dimethyltransferase 1, TFB1M, CGI-75, CGI75, mtTFB.

    • 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 MQAAKQLSQN FLLDLRLTDK IVRKAGNLTN AYVYEVGPGP GGITRSILNA DVAELLVVEK DTRFIPGLQM LSDAAPGKLR IVHGDVLTFK VEKAFSESLK RPWEDDPPNV HIIGNLPFSV STPLIIKWLE NISCRDGPFV YGRTQMTLTF QKEVAERLAA NTGSKQRSRL SVMAQYLCNV RHIFTIPGQA FVPKPEVDVG VVHFTPLIQP KIEQPFKLVE KVVQNVFQFR RKYCHRGLRM LFPEAQRLES TGRLLELADI DPTLRPRQLS ISHFKSLCDV YRKMCDEDPQ LFAYNFREEL KRRKSKNEEK EEDDAENYRL.

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    Tfb1M Human
  • View Data Sheet

    Name :

    TNC Rabbit

    Description:

    Skeletal Muscle Troponin-C Rabbit

    Troponin C skeletal muscle, TNNC2, TNC.

    Product # :

    PRO-323

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    Description

    Rabbit Skeletal Muscle Troponin-C is a single, glycosylated, polypeptide chain having a molecular mass of 18kDa. Troponin-C is one of three subunits that form the Troponin complex of striated muscle thin filaments. Skeletal muscle Troponin-C is purified using a combination of ion-exchange and affinity chromatography steps.

    Source

    Rabbit Skeletal Muscle.

    Formulation

    The Troponin C Rabbit protein solution contains 150mM sodium chloride, 10mM sodium phosphate and 0.05% sodium azide, pH-7.2.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

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    • Synonyms

      Troponin C skeletal muscle, TNNC2, TNC.

    • 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. Avoid multiple 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.

    Tnnc2 Rabbit
  • View Data Sheet

    Name :

    BMPR1A Human, CHO

    Description:

    Bone Morphogenetic Protein Receptor-1A Human Recombinant, CHO

    BMPR-1A, BMP-R1A, BMPR1A, BMR1A, CD292, CD-292, Serine/threonine-protein kinase receptor R5, SKR5, ALK-3, ACVRLK3, EC 2.7.11.30, CD292 antigen.

    Product # :

    CYT-1094

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    Description

    Bone Morphogenetic Protein Receptor-1A Human Recombinant produced in CHO cells is a glycosylated homodimer chain containing 2x362 amino acids and having a total molecular mass of 80.8kDa. BMPR1A is purified by proprietary chromatographic techniques.

    Source

    CHO cells.

    Formulation

    The protein was lyophilized from a sterile (0.2µm) filtered solution containing PBS.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50, as calculated by the Inhibition of human BMP-4-induced alkaline phosphatase production caused by ATDC5 cells is 120ng/ml corresponding to a specific activity of 8.3x10^3 units/mg.

    More Info

    • Introduction

      The bone morphogenetic protein (BMP) receptors are a family of transmembrane serine/threonine kinases that include the type I receptors BMPR1A and BMPR1B and the type II receptor BMPR2. These receptors are also closely related to the receptors, ACVR1 and ACVR2. The ligands of these receptors are members of the TGF-beta superfamily. TGF-betas transduce their signals through the formation of heteromeric complexes with 2 different types of serine (threonine) kinase receptors: type I receptors of about 50-55 kD and type II receptors of about 70-80 kD. Type II receptors bind ligands in the absence of type I receptors, but they require their respective type I receptors for signaling, whereas type I receptors require their respective type II receptors for ligand binding.

    • Synonyms

      BMPR-1A, BMP-R1A, BMPR1A, BMR1A, CD292, CD-292, Serine/threonine-protein kinase receptor R5, SKR5, ALK-3, ACVRLK3, EC 2.7.11.30, CD292 antigen.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized BMPR1A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BMPR1A 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 BMPR1A in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      QNLDSMLHGT GMKSDSDQKK SENGVTLAPE DTLPFLKCYC SGHCPDDAIN NTCITNGHCF AIIEEDDQGE TTLASGCMKY EGSDFQCKDS PKAQLRRTIE CCRTNLCNQY LQPTLPPVVI GPFFDGSIRI EGRMDDKTHT CPPCPAPELL GGPSVFLFPP KPKDTLMISR TPEVTCVVVD VSHEDPEVKF NWYVDGVEVH NAKTKPREEQ YNSTYRVVSV LTVLHQDWLN GKEYKCKVSN KALPAPIEKT ISKAKGQPRE PQVYTLPPSR DELTKNQVSL TCLVKGFYPS DIAVEWESNG QPENNYKTTP PVLDSDGSFF LYSKLTVDKS RWQQGNVFSC SVMHEALHNH YTQKSLSLSP GK.

    • Background

      Research Paper on Bone Morphogenetic Protein Receptor-1A Human Recombinant, CHO, Monomer, HEK

      Abstract:

      Welcome to the captivating world of Bone Morphogenetic Protein Receptor-1A Human Recombinant, CHO, Monomer (BMPR-1A HR) in Human Embryonic Kidney Cells (HEK). This research paper explores the vital role of BMPR-1A HR in cellular responses. As a key receptor in the transforming growth factor-beta (TGF-β) superfamily, BMPR-1A HR plays a significant part in guiding cellular differentiation and tissue development. Join us as we unravel the molecular mechanisms behind BMPR-1A HR signaling in HEK cells and delve into its interactions with key cytokines, including Tumor Necrosis Factor-alpha (TNF-α) and Tumor Necrosis Factor-alpha Superfamily Member 2 (TNFα SF2 or TNFSF2).

      Introduction:

      Welcome to the intriguing world of BMPR-1A HR! In this section, we introduce the remarkable BMPR-1A HR and its crucial role in shaping cellular responses. Together, let's explore how this receptor influences cellular behavior and contributes to tissue growth, fostering our understanding of its importance in biological processes.

      BMPR-1A HR Signaling in HEK Cells:

      Be amazed by the intricate dance of BMPR-1A HR signaling within HEK cells! Uncover the complex process of ligand-receptor binding, initiating both the canonical SMAD-dependent and non-canonical SMAD-independent pathways. This harmonious interplay regulates a wide range of cellular processes, including gene transcription, cell proliferation, and differentiation, forming the foundation of cellular communication.

      Influential Role in Cellular Responses:

      Marvel at the influential role of BMPR-1A HR as a critical mediator of cellular responses within HEK cells. Witness its ability to modulate cellular differentiation, driving the expression of key differentiation markers such as DIF. Our exploration will highlight the multifaceted nature of BMPR-1A HR, impacting diverse cellular pathways, including those involving TNF-α and TNFSF2, shaping a dynamic and interconnected cellular network.

      Interplay with Key Cytokines:

      Discover the intriguing interactions between BMPR-1A HR and key cytokines like TNF-α and TNFSF2. Explore how BMPR-1A HR influences their expression and activity, hinting at potential cross-talk between BMPR-1A HR and inflammatory pathways. This delicate balance fosters a harmonious cellular environment, where multiple players contribute to overall cellular responses.

      Therapeutic Implications and Tissue Development:

      Witness the potential therapeutic implications of BMPR-1A HR in tissue development. Together, we explore the exciting possibilities of utilizing BMPR-1A HR in regenerative medicine, offering hope for enhanced tissue development and repair. As we venture forth, we also address challenges, such as optimal dosage, innovative delivery methods, and safety considerations, ensuring a responsible and effective approach.

      Conclusion:

      As we conclude our exploration of BMPR-1A HR in HEK cells, we stand in awe of its role in mediating cellular responses and tissue development. Equipped with this knowledge, we look forward to a promising future, where BMPR-1A HR from CHO cells opens doors to innovative applications in regenerative medicine, contributing to improved human health and well-being.

      What is the molecular weight/Mw of BMPR1A Protein?
      BMPR1A Protein has a total Mw of 80.8kDa.

      What is the source or expression system of BMPR1A Protein?
      CHO cells.

      What is the Purity of BMPR1A Protein?
      BMPR1A Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of BMPR1A Protein?
      The ED50, as calculated by the Inhibition of human BMP-4-induced alkaline phosphatase production caused by ATDC5 cells is 120ng/ml corresponding to a specific activity of 8.3x10^3 units/mg.

      What is the amino acid sequence of BMPR1A Protein?
      QNLDSMLHGT GMKSDSDQKK SENGVTLAPE DTLPFLKCYC SGHCPDDAIN NTCITNGHCF AIIEEDDQGE TTLASGCMKY EGSDFQCKDS PKAQLRRTIE CCRTNLCNQY LQPTLPPVVI GPFFDGSIRI EGRMDDKTHT CPPCPAPELL GGPSVFLFPP KPKDTLMISR TPEVTCVVVD VSHEDPEVKF NWYVDGVEVH NAKTKPREEQ YNSTYRVVSV LTVLHQDWLN GKEYKCKVSN KALPAPIEKT ISKAKGQPRE PQVYTLPPSR DELTKNQVSL TCLVKGFYPS DIAVEWESNG QPENNYKTTP PVLDSDGSFF LYSKLTVDKS RWQQGNVFSC SVMHEALHNH YTQKSLSLSP GK.

      What applications can BMPR1A Protein be used in?
      BMPR1A Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for BMPR1A Protein?
      The endotoxin level is minimal, BMPR1A 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.

    Bmpr1A Protein
  • View Data Sheet

    Name :

    MOBKL3 Human

    Description:

    MOB1, Mps One Binder kinase Activator-Like 3 Human Recombinant

    Mps one binder kinase activator-like 3, 2C4D, Class II mMOB1, Mob1 homolog 3, Mob3, Preimplantation protein 3, MOBKL3, MOB3, PREI3, MOB1, PREI3, CGI-95, MGC12264.

    Product # :

    PRO-049

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    Description

    MOBKL3 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 245 amino acids (1-225 a.a.) and having a molecular mass of 28.1kDa. The MOBKL3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The MOBKL3 solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH8.0) containing 0.2M Nacl, 5mM DTT, 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Mps one binder kinase activator-like 3 (MOBKL3) is a member of the MOB1/Phocein family and is phosphorylated on serine residues. MOBKL3 is usually linked with membranes but can be present in the cytosol, where it behaves as a protein complex. MOBKL3 is the major partner of the striatin family members, which are scaffolding proteins involved in signaling and trafficking.

    • Synonyms

      Mps one binder kinase activator-like 3, 2C4D, Class II mMOB1, Mob1 homolog 3, Mob3, Preimplantation protein 3, MOBKL3, MOB3, PREI3, MOB1, PREI3, CGI-95, MGC12264.

    • 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 MVMAEGTAVL RRNRPGTKAQ DFYNWPDESF DEMDSTLAVQ QYIQQNIRAD CSNIDKILEP PEGQDEGVWK YEHLRQFCLE LNGLAVKLQS ECHPDTCTQM TATEQWIFLC AAHKTPKECP AIDYTRHTLD GAACLLNSNK YFPSRVSIKE SSVAKLGSVC RRIYRIFSHA YFHHRQIFDE YENETFLCHR FTKFVMKYNL MSKDNLIVPI LEEEVQNSVS GESEA.

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    Mobkl3 Human
  • View Data Sheet

    Name :

    Colloidal Gold

    Description:

    Colloidal Gold 40nM 2OD

    Product # :

    PRO-2830

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    Description

    Gold nanoparticles have one-of-a-kind properties turn them to ideal for detecting even the smallest amounts of biological molecules. These particles can be loaded with drugs or other therapeutic agents and then targeted to specific cells/tissues. Further to their diagnostic applications, gold nanoparticles may also take part in drug delivery and cancer therapy. Colloidal Gold is purified by proprietary chromatographic techniques.

    Formulation

    Colloidal Gold solution (6.7mg/ml) contains 50mM sodium citrate.

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    • Physical Appearance

      Sterile Filtered red solution.

    • Stability

      Colloidal Gold should be stored at 4°C, DO NOT FREEZE.

    • Background

      Colloidal gold is liquid form colloid nanoparticles of gold in a water. The colloidal gold color is dependent of the particle size, below 100 nm gives a is deep purple red color due to the spherical nanoparticles. Colloid gold is crucial for research due to its unique properties such as electronic charge, Mw and optical properties. Colloid gold is used in biomedical devices, electron microscopy and nanotechnology.

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    Colloidal Gold
  • View Data Sheet

    Name :

    PITPNA Human

    Description:

    Phosphatidylinositol Transfer Protein Alpha Human Recombinant

    Phosphatidylinositol transfer protein alpha isoform, PI-TP-alpha, PtdIns transfer protein alpha, PtdInsTP alpha, PITPNA, PITPN, VIB1A, MGC99649, PI-TPalpha.

    Product # :

    PRO-044

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    Description

    PITPNA Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 290 amino acids (1-270 a.a.) and having a molecular mass of 33.9kDa. The PITPNA is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PITPNA solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol, 1mM EDTA.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Phosphatidylinositol transfer protein alpha (PITPNA) is found in the cytoplasm, where it catalyzes the transfer of phosphatidylinositol (PI) and phosphatidylcholine (PC) between membranes. PITPNA belongs to a family of lipid-binding proteins which transfer molecules of phosphatidylinositol or phosphatidylcholine between membrane surfaces. PITPNA is implicated in phospholipase C signaling and in the production of phosphatidylinositol 3, 4, 5-trisphosphate (PIP3) by phosphoinositide-3-kinase.

    • Synonyms

      Phosphatidylinositol transfer protein alpha isoform, PI-TP-alpha, PtdIns transfer protein alpha, PtdInsTP alpha, PITPNA, PITPN, VIB1A, MGC99649, PI-TPalpha.

    • 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 MVLLKEYRVI LPVSVDEYQV GQLYSVAEAS KNETGGGEGV EVLVNEPYEK DGEKGQYTHK IYHLQSKVPT FVRMLAPEGA LNIHEKAWNA YPYCRTVITN EYMKEDFLIK IETWHKPDLG TQENVHKLEP EAWKHVEAVY IDIADRSQVL SKDYKAEEDP AKFKSIKTGR GPLGPNWKQE LVNQKDCPYM CAYKLVTVKF KWWGLQNKVE NFIHKQERRL FTNFHRQLFC WLDKWVDLTM DDIRRMEEET KRQLDEMRQK DPVKGMTADD.

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    Pitpna Human
  • View Data Sheet

    Name :

    NEFL Bovine

    Description:

    Neurofilament Light Bovine

    Neurofilament light polypeptide, NF-L, NEFL, NF68, NFL, 68 kDa neurofilament protein.

    Product # :

    PRO-2786

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    Description

    NEFL Bovine having a calculated molecular mass of 68 kDa, pI-5.0.

    Source

    Bovine spinal cord.

    Formulation

    NEFL was lyophilized from a 1mg/ml solution containing 10mM sodium phosphate buffer pH 7.5, 6M urea, 1mM EDTA, 2mM DTT and 10mM methylammonium chloride.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Synonyms

      Neurofilament light polypeptide, NF-L, NEFL, NF68, NFL, 68 kDa neurofilament protein.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store the lyophilized NEFL between 2-8°C, do not freeze. Upon reconstitution NEFL should be stored at -20°C.Please prevent freeze-thaw cycles.

    • Solubility

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

    • Background

      Neurofilament light chain (NEFL) is a critical component of the neuronal cytoskeleton, primarily found in neurons of the central and peripheral nervous systems. While extensive research has been conducted on NEFL in human and rodent models, the study of NEFL in bovine nervous tissues is an emerging area with potential for advancing our understanding of neuronal biology in larger mammals and its applications in veterinary medicine and neurobiology.

      Bovine nervous tissues, such as the brain and spinal cord, are of particular interest due to their relevance in cattle health and the food industry. This research aims to provide a comprehensive exploration of NEFL in bovine nervous tissues, elucidating its functions, structural significance, and potential applications.

      The primary objective of this research is to elucidate the role of NEFL in bovine nervous tissues, particularly in maintaining the structural integrity of neurons and axons. In vitro and ex vivo experiments, utilizing bovine neuronal cell cultures and tissue specimens, will be conducted to investigate how NEFL contributes to neuronal morphology, axonal transport, and neuronal resilience. Understanding these mechanisms is fundamental for deciphering the complexities of neuronal biology in bovine species.

      The second objective is to assess the relevance of bovine NEFL in veterinary medicine. Studies involving bovine models will be conducted to evaluate the impact of NEFL mutations or variations on neuronal health, disease susceptibility, and neurodegenerative conditions. These investigations may provide valuable insights into potential applications in cattle health and the development of diagnostic tools for neurological disorders.

      The third objective is to explore the potential applications of bovine NEFL in neurobiology and biotechnology. Research will investigate the use of bovine NEFL-expressing cells as models for studying neuronal-related diseases and for developing tissue engineering approaches for veterinary medicine and biotechnology.

      By delving into the functions and roles of NEFL in bovine nervous tissues, this research aims to expand our knowledge of neuronal biology, its implications for veterinary medicine, and its potential applications in neurobiology and cattle health

    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.

    Nefl Bovine
  • View Data Sheet

    Name :

    SEMG1 Human

    Description:

    Semenogelin I Human Recombinant

    CT103, dJ172H20.2, SEMG, SGI, Semenogelin-1, Semenogelin I, SEMG1.

    Product # :

    PRO-1732

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    Description

    SEMG1 Human Recombinant produced in E. coli is a single polypeptide chain containing 462 amino acids (24-462) and having a molecular mass of 52kDa. SEMG1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SEMG1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 7.5), 0.5M NaCl, 10% glycerol, 250mM Imidazole, 0.1mM PMSF and 1mM DTT.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      SEMG1 is the predominant protein in semen. The secreted protein takes part in the formation of a gel matrix which encases ejaculated spermatozoa. The prostate-specific antigen (PSA) protease processes SEMG1 into smaller peptides, with each possibly having a separate function. The proteolysis process breaks down the gel matrix and allows the spermatozoa to shift more freely. 2 transcript variants encoding different isoforms have been found for SEMG1.

    • Synonyms

      CT103, dJ172H20.2, SEMG, SGI, Semenogelin-1, Semenogelin I, SEMG1.

    • 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 MGSQKGGSKG RLPSEFSQFP HGQKGQHYSG QKGKQQTESK GSFSIQYTYH VDANDHDQSR KSQQYDLNAL HKTTKSQRHL GGSQQLLHNK QEGRDHDKSK GHFHRVVIHH KGGKAHRGTQ NPSQDQGNSP SGKGISSQYS NTEERLWVHG LSKEQTSVSG AQKGRKQGGS QSSYVLQTEE LVANKQQRET KNSHQNKGHY QNVVEVREEH SSKVQTSLCP AHQDKLQHGS KDIFSTQDEL LVYNKNQHQT KNLNQDQQHG RKANKISYQS SSTEERRLHY GENGVQKDVS QSSIYSQTEE KAQGKSQKQI TIPSQEQEHS QKANKISYQS SSTEERRLHY GENGVQKDVS QRSIYSQTEK LVAGKSQIQA PNPKQEPWHG ENAKGESGQS TNREQDLLSH EQKGRHQHGS HGGLDIVIIE QEDDSDRHLA QHLNNDRNPL FT.

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    Semg1 Human
  • View Data Sheet

    Name :

    SPARC Mouse

    Description:

    Secreted Protein Acidic & Rich in Cysteine Mouse Recombinant

    Osteonectin, ON, Basement-membrane protein 40, BM-40, SPARC, Secreted Protein acidic and Rich in Cysteine

    Product # :

    PRO-2658

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    Description

    SPARC Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 291 amino acids (18-302a.a) and having a molecular mass of 33.3kDa.SPARC is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

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    • Introduction

      Secreted Protein Acidic & Rich in Cysteine (SPARC) protein is coded by the SPARC gene in humans. SPARC is a glycoprotein located in bones that binds to calcium. SPARC is produced by fibroblasts, capillary endothelial cells, platelets and macrophages, mainly in areas of tissue morphogenesis and remodelling. Asides from calcium, SPARC can also bind to collagen.

    • Synonyms

      Osteonectin, ON, Basement-membrane protein 40, BM-40, SPARC, Secreted Protein acidic and Rich in Cysteine

    • 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

      APQQTEVAEE IVEEETVVEE TGVPVGANPV QVEMGEFEDG AEETVEEVVA DNPCQNHHCK HGKVCELDES NTPMCVCQDP TSCPAPIGEF EKVCSNDNKT FDSSCHFFAT KCTLEGTKKG HKLHLDYIGP CKYIAPCLDS ELTEFPLRMR DWLKNVLVTL YERDEGNNLL TEKQKLRVKK IHENEKRLEA GDHPVELLAR DFEKNYNMYI FPVHWQFGQL DQHPIDGYLS HTELAPLRAP LIPMEHCTTR FFETCDLDND KYIALEEWAG CFGIKEQDIN KDLVIHHHHH H

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    Sparc Mouse
  • View Data Sheet

    Name :

    SRP19 Human

    Description:

    Signal Recognition Particle 19kDa Human Recombinant

    Signal recognition particle 19kDa protein, SRP19.

    Product # :

    PRO-1474

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    Description

    SRP19 Human Recombinant fused with a 23 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 167 amino acids (1-144 a.a.) and having a molecular mass of 18.5kDa. The SRP19 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SRP19 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 50% glycerol and 2mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Signal recognition particle 19kDa protein (SRP19) is a member of the SRP19 family. SRP19 binds directly to 7S RNA and mediates binding of the 54 kDa subunit of the SRP.

    • Synonyms

      Signal recognition particle 19kDa protein, SRP19.

    • 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 MGSMACAAAR SPADQDRFIC IYPAYLNNKK TIAEGRRIPI SKAVENPTAT EIQDVCSAVG LNVFLEKNKM YSREWNRDVQ YRGRVRVQLK QEDGSLCLVQ FPSRKSVMLY AAEMIPKLKT RTQKTGGADQ SLQQGEGSKK GKGKKKK.

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    Srp19 Human
  • View Data Sheet

    Name :

    COPS7A Human

    Description:

    COP9 Signalosome Subunit 7A Human Recombinant

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

    Product # :

    PRO-1947

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

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

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

    Cops7A Human
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