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1000 results found for “Nucleobindin”
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Name :
S100B Human, HisDescription:
S100 Calcium Binding Protein B Human Recombinant, His Tag
Protein S100-B, S100 calcium-binding protein B, S-100 protein subunit beta, S-100 protein beta chain, S100B, NEF, S100, S100beta.
Product # :
PRO-306Price :
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Shipped with Ice Packs
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Description
S100B Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 112 amino acids fragment (1-92) with a 20 amino acids N-terminal His tag and having a total molecular mass of 12.8kDa. The S100B is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
S100B (1mg/ml) is supplied in 20mM Tris-HCl buffer (pH8.0), 1mM DTT and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
S100b is a member of the S100 family of proteins which are a family of EF-hand calcium binding proteins that exist mostly as dimers of the 20 currently identified individual S100 monomers. The S100B homodimer is expressed in cells of the central nervous system, glial cells and in certain peripheral cells e.g. Schwann cells, melanocytes, adipocytes and chondrocytes. S100 proteins are localized either in the cytoplasm or the nucleus of a wide range of cells. S100 proteins are involved in the regulation of a number of cellular processes such as cell cycle progression and differentiation. There are at least 13 members in the S100 gene family, which are located as a cluster on chromosome 1q21; however, S100b is located at 21q22.3. The determination of S100B in serum levels may be used to monitor the extent of brain injury and malignant melanoma. S100b proteins may have a role in Neurite extension, proliferation of melanoma cells, stimulation of Ca2+ fluxes, inhibition of PKC-mediated phosphorylation, astrocytosis and axonal proliferation, and inhibition of microtubule assembly. Chromosomal rearrangements and altered expression of the S100b gene are implicated in several neurological, neoplastic, and other types of diseases, including Alzheimer's disease, Down's syndrome, epilepsy, amyotrophic lateral sclerosis, melanoma, and type I diabetes.
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Synonyms
Protein S100-B, S100 calcium-binding protein B, S-100 protein subunit beta, S-100 protein beta chain, S100B, NEF, S100, S100beta.
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Physical Appearance
Sterile Filtered clear solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSELEKAMVA LIDVFHQYSG REGDKHKLKK SELKELINNE LSHFLEEIKE QEVVDKVMET LDNDGDGECD FQEFMAFVAM VTTACHEFFE HE.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
HINT1 HumanDescription:
Histidine Triad Nucleotide Binding Protein 1 Human Recombinant
HINT, PKCI-1, PRKCNH1, FLJ30414, FLJ32340, HINT1, Histidine triad nucleotide-binding protein 1, Adenosine 5'-monophosphoramidase, Protein kinase C inhibitor 1, Protein kinase C-interacting protein 1, PKCI1.
Product # :
PRO-702Price :
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Description
HINT1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 126 amino acids (1-126 a.a.) and having a molecular mass of 13.8 kDa.The HINT1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The HINT1 solution contains 20mM Tris pH-8 & 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
HINT1, also known as Histidine triad nucleotide-binding protein 1 is part of the superfamily named for a near C-terminal HXHXHXX motif (H:Histidine, X:a hydrophobic amino acid) positioned at the ?-phosphate of nucleotide substrates. HINT1 hydrolyzes adenosine 5'-monophosphoramidate substrates such as AMP-morpholidate, AMP-N-alanine methyl ester, AMP-alpha-acetyl lysine methyl ester and AMP-NH2. Though it was initially considered to be a protein kinase C inhibitor and act as a haplod-insufficient tumor suppressor including spontaneous tumor formation in Hint+/- and Hint-/- , its actual physiologic function is not known.
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Synonyms
HINT, PKCI-1, PRKCNH1, FLJ30414, FLJ32340, HINT1, Histidine triad nucleotide-binding protein 1, Adenosine 5'-monophosphoramidase, Protein kinase C inhibitor 1, Protein kinase C-interacting protein 1, PKCI1.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MADEIAKAQV ARPGGDTIFG KIIRKEIPAK IIFEDDRCLA FHDISPQAPT HFLVIPKKHI SQISVAEDDD ESLLGHLMIV GKKCAADLGL NKGYRMVVNE GSDGGQSVYH VHLHVLGGRQ MHWPPG.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
MYOZ1 HumanDescription:
Myozenin 1 Human Recombinant
CS-2, FATZ, MYOZ, Calsarcin-2, Filamin-, actinin- and telethonin-binding protein,Protein FATZ, MYOZ1.
Product # :
PRO-1652Price :
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Description
MYOZ1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 322 amino acids (1-299 a.a.) and having a molecular mass of 34.1kDa.MYOZ1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MYOZ1 protein solution (1mg/ml) contains 20mM Tris-HCl buffer, (pH 8.0), 0.4M UREA and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Myozenin 1 (MYOZ1) is a member of the myozenin family. MYOZ1 is mostly expressed in the skeletal muscle. Members of the myozenin family act as calcineurin-interacting proteins which helps tether calcineurin to the sarcomere of cardiac and skeletal muscle. The myozenin family plays a significant role in modulation of calcineurin signaling.
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Synonyms
CS-2, FATZ, MYOZ, Calsarcin-2, Filamin-, actinin- and telethonin-binding protein,Protein FATZ, MYOZ1.
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Physical Appearance
Sterile Filtered clear solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMPLSGTP APNKKRKSSK LIMELTGGGQ ESSGLNLGKK ISVPRDVMLE ELSLLTNRGS KMFKLRQMRV EKFIYENHPD VFSDSSMDHF QKFLPTVGGQ LGTAGQGFSY SKSNGRGGSQ AGGSGSAGQY GSDQQHHLGS GSGAGGTGGP AGQAGRGGAA GTAGVGETGS GDQAGGEGKH ITVFKTYISP WERAMGVDPQ QKMELGIDLL AYGAKAELPK YKSFNRTAMP YGGYEKASKR MTFQMPKFDL GPLLSEPLVL YNQNLSNRPS FNRTPIPWLS SGEPVDYNVD IGIPLDGETE EL.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
NACA HumanDescription:
Nascent Polypeptide-Associated Complex Alpha Human Recombinant
Nascent polypeptide-associated complex alpha subunit, NACA1, NAC-alpha, alpha-NAC, Allergen Hom s 2.
Product # :
PRO-974Price :
Quantity :
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Description
NACA Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 235 amino acids (1-215) and having a molecular mass of 25.5 kDa.NACA is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The NACA solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
NACA belongs to the nascent polypeptide associated complex (NAC) alpha subunit family which takes part in inhibiting unsuitable targeting of non-secretory polypeptides to the endoplasmic reticulum (ER). NACA proteins are usually restricted to the nucleus and cytoplasm and hold NAC-A/B (NAC-alpha/beta) and UBA (ubiquitin-associated) domains. The UBA domain is related to proteins which takes part in the ubiquitin-proteasome pathway for protein degradation.
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Synonyms
Nascent polypeptide-associated complex alpha subunit, NACA1, NAC-alpha, alpha-NAC, Allergen Hom s 2.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MPGEATETVP ATEQELPQPQ AETGSGTESD SDESVPELEE QDSTQATTQQ AQLAAAAEID EEPVSKAKQS RSEKKARKAM SKLGLRQVTG VTRVTIRKSK NILFVITKPD VYKSPASDTY IVFGEAKIED LSQQAQLAAA EKFKVQGEAV SNIQENTQTP TVQEESEEEE VDETGVEVKD IELVMSQANV SRAKAVRALK NNSNDIVNAI MELTM
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
NUDT14 HumanDescription:
Nudix Type Motif 14 Human Recombinant
UGPP, UGPPase, Uridine diphosphate glucose pyrophosphatase, UDPG pyrophosphatase, Nucleoside diphosphate-linked moiety X motif 14, Nudix motif 14, NUDT14.
Product # :
ENZ-691Price :
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Description
NUDT14 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 245 amino acids (1-222) and having a molecular mass of 26.5kDa. NUDT14 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The NUDT14 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Uridine diphosphate glucose pyrophosphatase (NUDT14), is a part of the nudix hydrolase family. NUDT14 is a cytoplasmic protein which contains one nudix hydrolase domain and acts as the sugar donor in numerous glycosylation reactions, including those involved in the production of glycogen. NUDT14 hydrolyzes ADP-ribose into ribose 5-phosphate and AMP, and UDP-glucose to glucose 1-phosphate and UMP. NUDT14 is a homodimer which binds magnesium as a cofactor and is encoded by a gene located on human chromosome 14.
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Synonyms
UGPP, UGPPase, Uridine diphosphate glucose pyrophosphatase, UDPG pyrophosphatase, Nucleoside diphosphate-linked moiety X motif 14, Nudix motif 14, NUDT14.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMERIEGA SVGRCAASPY LRPLTLHYRQ NGAQKSWDFM KTHDSVTVLL FNSSRRSLVL VKQFRPAVYA GEVERRFPGS LAAVDQDGPR ELQPALPGSA GVTVELCAGL VDQPGLSLEE VACKEAWEEC GYHLAPSDLR RVATYWSGVG LTGSRQTMFY TEVTDAQRSG PGGGLVEEGE LIEVVHLPLE GAQAFADDPD IPKTLGVIFG VSWFLSQVAP NLDLQ.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
PA2G4 HumanDescription:
Proliferation-associated protein 2G4 Human Recombinant
Proliferation-associated protein 2G4, Cell cycle protein p38-2G4 homolog, hG4-1, ErbB3-binding protein 1, PA2G4, EBP1, p38-2G4.
Product # :
PRO-782Price :
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Shipped with Ice Packs
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Description
PA2G4 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 402 amino acids (1-394 a.a.) and having a molecular mass of 44.8kDa. PA2G4 is fused to 8 amino acids His Tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PA2G4 protein solution contains 20mM Tris-HCl buffer (pH8.0) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
PA2G4 belongs to the peptidase M24C family and functions as an RNA-binding protein involved in cellular proliferation and differentiation processes. PA2G4 is a component of pre-ribosomal ribonucleoprotein complexes, participating in ribosome assembly and regulating the later steps of rRNA processing. Also, PA2G4 interacts with ErbB-3 and may function as a modulator of the ErbB-3 mediated signal transduction pathway by regulating the effects of Neuregulin-1. Furthermore, PA2G4 is a transcriptional co-repressor of androgen receptor-regulated genes and other cell cycle regulatory genes through its interactions with histone deacetylases. PA2G4 is implicated in growth inhibition and the induction of differentiation of human cancer cells. In addition, PA2G4 mediates cap-independent translation of specific viral IRESs (internal ribosomal entry site). PA2G4 associates with 28S, 18S and 5.8S mature rRNAs, several rRNA precursors and probably U3 small nucleolar RNA.
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Synonyms
Proliferation-associated protein 2G4, Cell cycle protein p38-2G4 homolog, hG4-1, ErbB3-binding protein 1, PA2G4, EBP1, p38-2G4.
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Physical Appearance
Sterile filtered colorless solution.
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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.
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Amino Acid Sequence
MSGEDEQQEQ TIAEDLVVTK YKMGGDIANR VLRSLVEASS SGVSVLSLCE KGDAMIMEET GKIFKKEKEM KKGIAFPTSI SVNNCVCHFS PLKSDQDYIL KEGDLVKIDL GVHVDGFIAN VAHTFVVDVA QGTQVTGRKA DVIKAAHLCA EAALRLVKPG NQNTQVTEAW NKVAHSFNCT PIEGMLSHQL KQHVIDGEKT IIQNPTDQQK KDHEKAEFEV HEVYAVDVLV SSGEGKAKDA GQRTTIYKRD PSKQYGLKMK TSRAFFSEVE RRFDAMPFTL RAFEDEKKAR MGVVECAKHE LLQPFNVLYE KEGEFVAQFK FTVLLMPNGP MRITSGPFEP DLYKSEMEVQ DAELKALLQS SASRKTQKKK KKKASKTAEN ATSGETLEEN EAGDLEHHHH HH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
C4BPB HumanDescription:
Complement Component 4 Binding Protein, Beta Human Recombinant
C4b-binding protein beta chain, C4BPB, C4BP.
Product # :
PRO-1174Price :
Quantity :
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Shipped with Ice Packs
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Description
C4BPB Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 260 amino acids (18-252 a.a) and having a molecular mass of 29kDa.C4BPB is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
C4BPB protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0) and 10% glycerol and 0.15M NaCl.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Complement Component 4 Binding Protein, Beta (C4BPB) belongs to a superfamily of proteins composed primarily of tandemly arrayed short consensus repeats of approximately 60 amino acids. C4BPB has a regulatory role in the coagulation system also, mediated via the beta-chain binding of protein S, a vitamin K-dependent protein which functions as a cofactor of activated protein C. A single, unique beta-chain of the C4BPB assembles with 7 identical alpha-chains into the principal isoform of C4BPB, which is a multimeric protein that controls activation of the complement cascade via the classical pathway. C4BPB binds as a cofactor to C3b/C4b inactivator (C3bINA), which subsequently hydrolyzes the complement fragment C4b. In addition, C4BPB accelerates the degradation of the C4bC2a complex (C3 convertase) by detaching the complement fragment C2a. Furthermore, C4BPB interacts with anticoagulant protein S and with serum amyloid P component.
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Synonyms
C4b-binding protein beta chain, C4BPB, C4BP.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMSDAEH CPELPPVDNS IFVAKEVEGQ ILGTYVCIKG YHLVGKKTLF CNASKEWDNT TTECRLGHCP DPVLVNGEFS SSGPVNVSDK ITFMCNDHYI LKGSNRSQCL EDHTWAPPFP ICKSRDCDPP GNPVHGYFEG NNFTLGSTIS YYCEDRYYLV GVQEQQCVDG EWSSALPVCK LIQEAPKPEC EKALLAFQES KNLCEAMENF MQQLKESGMT MEELKYSLEL KKAELKAKLL.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
PKIB HumanDescription:
Protein Kinase Inhibitor Beta Human Recombinant
cAMP-dependent protein kinase inhibitor beta, PKI-beta, PKIB, PRKACN2, FLJ23817.
Product # :
PKA-003Price :
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Description
PKIB Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 98 amino acids (1-78) and having a molecular mass of 10.6kDa (Molecular size on SDS-PAGE will appear higher). PKIB is fused to a 20 aa His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PKIB solution (1mg/ml) 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
cAMP-dependent protein kinase inhibitor beta (PKIB) belongs to the cAMP-dependent protein kinase inhibitor family. PKIB may interact with the catalytic subunit of cAMP-dependent protein kinase and function as a competitive inhibitor.
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Synonyms
cAMP-dependent protein kinase inhibitor beta, PKI-beta, PKIB, PRKACN2, FLJ23817.
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Physical Appearance
Sterile filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MRTDSSKMTD VESGVANFAS SARAGRRNAL PDIQSSAATD GTSDLPLKLE ALSVKEDAKE KDEKTTQDQL EKPQNEEK.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
PNOC HumanDescription:
Prepronociceptin Human Recombinant
Prepronociceptin, Nocistatin, OFQ, Pre-Pro-N/OFQ, Pronociceptin, Orphanin FQ, Nociceptin, PpN/OFQ, N/OFQ, PPNOC.
Product # :
PRO-1442Price :
Quantity :
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Shipped with Ice Packs
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Description
PNOC Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 180 amino acids (20-176) and having a molecular mass of 20.6kDa. PNOC is fused to a 23 amino acid His-tag at N-terminus.
Source
Escherichia Coli.
Formulation
PNOC protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Prepronociceptin (PNOC) is the ligand of the opioid receptor-like receptor (OPRL1). PNOC functions as a transmitter in the brain by modulating nociceptive and locomotor behavior. The PNOC protein may also be involved in neuronal differentiation and development.
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Synonyms
Prepronociceptin, Nocistatin, OFQ, Pre-Pro-N/OFQ, Pronociceptin, Orphanin FQ, Nociceptin, PpN/OFQ, N/OFQ, PPNOC.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSSCQRDCL TCQEKLHPAL DSFDLEVCIL ECEEKVFPSP LWTPCTKVMA RSSWQLSPAA PEHVAAALYQ PRASEMQHLR RMPRVRSLFQ EQEEPEPGME EAGEMEQKQL QKRFGGFTGA RKSARKLANQ KRFSEFMRQY LVLSMQSSQR RRTLHQNGNV.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CEBP Gamma HumanDescription:
CCAAT/enhancer binding protein C/EBP Gamma Recombinant Human
CCAAT/enhancer-binding protein gamma, C/EBP gamma, CEBPG, GPE1BP, IG/EBP-1.
Product # :
PRO-434Price :
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Description
CEBP-g Recombinant Human His-Tag fusion protein produced in E.Coli is a single, non-glycosylated polypeptide chain containing amino acids 146 (aa 39-147) and having a molecular mass of 16.5 kDa. The DNA binding domain of CEBP-g was purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein contains 20mM Tris-HCl pH7.5, 0.1M NaCl and 5mM b-Mercaptoethanol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
CCAAT/enhancer binding protein(C/EBP) g is a family of transcription factors all contain a highly conserved, basic-leucine zipper domain at the C-terminus that is involved in dimerization and DNA binding. C/EBP family of transcription factors regulates viral and cellular CCAAT/enhancer element-mediated transcription. C/EBP family consist of several related proteins, C/EBP a,b,g,d, that form homodimers and/or form heterodimers with each other. C/EBP proteins contain the bZIP region, which is characterized by two motifs in the C-terminal half of the protein; a basic region involved in DNA binding and a leucine zipper motif involved in dimerization. C/EBP g may cooperate with Fos to bind PRE- enhancer elements.
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Synonyms
CCAAT/enhancer-binding protein gamma, C/EBP gamma, CEBPG, GPE1BP, IG/EBP-1.
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Physical Appearance
Sterile filtered colorless solution.
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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.
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Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMPGG GGKAVAPSKQ SKKSSPMDRN SDEYRQRRER NNMAVKKSRL KSKQKAQDTL QRVNQLKEEN ERLEAKIKLL TKELSVLKDL FLEHAHNLAD NVQSISTENT TADGDN.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CIAPIN1 HumanDescription:
Cytokine Induced Apoptosis Inhibitor 1 Human Recombinant
DRE2, PRO0915, Anamorsin, Cytokine-induced apoptosis inhibitor 1, Fe-S cluster assembly protein DRE2 homolog, CIAPIN1.
Product # :
PRO-024Price :
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Description
CIAPIN1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 335 amino acids (1-312 a.a.) and having a molecular mass of 36kDa.CIAPIN1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CIAPIN1 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Anamorsin, ( CIAPIN) is a member of anamorsin family. CIAPIN mainly expressed in the cytoplasm of liver, pancreas and heart tissue cells and does not show any homology to known apoptosis regulatory molecules of the Bcl-2 or CASP families, or to signal transduction molecules. CIAPIN1 Expression is reliant on growth factor stimulation. It is a ubiquitously expressed protein, and when it is overexpressed, it grants apoptotic resistance.
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Synonyms
DRE2, PRO0915, Anamorsin, Cytokine-induced apoptosis inhibitor 1, Fe-S cluster assembly protein DRE2 homolog, CIAPIN1.
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Physical Appearance
Sterile Filtered clear solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMADFGIS AGQFVAVVWD KSSPVEALKG LVDKLQALTG NEGRVSVENI KQLLQSAHKE SSFDIILSGL VPGSTTLHSA EILAEIARIL RPGGCLFLKE PVETAVDNNS KVKTASKLCS ALTLSGLVEV KELQREPLTP EEVQSVREHL GHESDNLLFV QITGKKPNFE VGSSRQLKLS ITKKSSPSVK PAVDPAAAKL WTLSANDMED DSMDLIDSDE LLDPEDLKKP DPASLRAASC GEGKKRKACK NCTCGLAEEL EKEKSREQMS SQPKSACGNC YLGDAFRCAS CPYLGMPAFK PGEKVLLSDS NLHDA.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
RLN2 HumanDescription:
Relaxin-2 Human Recombinant
Prorelaxin H2, RLN2, H2, RLXH2, H2-RLX, bA12D24.1.1, bA12D24.1.2.
Product # :
PRO-1327Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
RLN2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 184 amino acids (25-185 a.a) and having a molecular mass of 20.7kDa.RLN2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
RLN2 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
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Introduction
Prorelaxin H2 (RLN2) is a member of a family which is produced by the ovary, targets the mammalian reproductive system to ripen the cervix, elongate the pubic symphysis and inhibit uterine contraction. It may also have other roles in boosting sperm motility, regulating blood pressure, controlling heart rate and releasing vasopressin. RLN2 is a peptide hormone linked to several therapeutically relevant physiological effects, including regulation of collagen metabolism and multiple vascular control pathways. The active form of the RLN2 protein consists of an A chain and a B chain linked by disulfide bonds.
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Synonyms
Prorelaxin H2, RLN2, H2, RLXH2, H2-RLX, bA12D24.1.1, bA12D24.1.2.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSDSWMEEV IKLCGRELVR AQIAICGMST WSKRSLSQED APQTPRPVAE IVPSFINKDT ETINMMSEFV ANLPQELKLT LSEMQPALPQ LQQHVPVLKD SSLLFEEFKK LIRNRQSEAA DSSPSELKYL GLDTHSRKKR QLYSALANKC CHVGCTKRSL ARFC.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
OSM Human, 209 a.aDescription:
Oncostatin M Human Recombinant (209 a.a.)
OSM, MGC20461, Oncostatin M.
Product # :
CYT-639Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Oncostatin-M (209 a.a.) Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 209 amino acids and having a molecular mass of 23.9kDa. The Oncostatin-M (209 a.a.) is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Oncostatin-M (209 a.a.) was lyophilized from a concentrated (1mg/ml) solution containing 1x PBS pH-7.4.
Purity
Greater than 97.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by the dose-dependant stimulation of Human TF-1 cells is < 2 ng/ml, corresponding to a Specific Activity of 500,000 IU/mg.More Info
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Introduction
Oncostatin M is a member of a cytokine family that includes leukemia-inhibitory factor, granulocyte colony-stimulating factor, and interleukin 6. This gene encodes a growth regulator which inhibits the proliferation of a number of tumor cell lines. It regulates cytokine production, including IL-6, G-CSF and GM-CSF from endothelial cells.
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Synonyms
OSM, MGC20461, Oncostatin M.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Oncostatin-M (209 a.a.) although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Oncostatin-M (209 a.a.) 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.
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Solubility
It is recommended to reconstitute the lyophilized Oncostatin-M (209 a.a.) in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
AAIGSCSKEYRVLLGQLQKQTDLMQDTSRLLDPYIRIQGLDVPKLREHCRERPG
AFPSEETLRGLGRRGFLQTLNATLGCVLHRLADLEQRLPKAQDLERSGLNIEDL
EKLQMARPNILGLRNNIYCMAQLLDNSDTAEPTKAGRGASQPPTPTPASDAFQ
RKLEGCRFLHGYHRFMHSVGRVFKWGESPNRSRRHSPHQALRKGVRR.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
s100bb HumanDescription:
s100bb Human homodimer
Product # :
PRO-2797Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
s100bb Human produced in Human brain tissue is suitable for use as a standard in immunoassay and as an immunogen for antiserum production.
Source
Human brain tissue.
Formulation
s100bb was lyophilized from 5mM Tris-HCl, pH 7.5, 2mM EDTA and 5mM 2-mercaptoethanol.
Purity
Greater than 95.0% .
More Info
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized s100bb homodimer although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution s100bb 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.
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Solubility
It is recommended to reconstitute the lyophilized s100bb in sterile 18MΩ-cm H2O containing 5mM 2- mercaptoethanol not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Background
S100BB is not only active in mature brains but also plays a significant role during brain development. It contributes to neural progenitor cell proliferation, neuronal migration, and differentiation. Studies have suggested that alterations in S100BB expression during development might influence the wiring of neural circuits, potentially impacting cognitive functions later in life. Investigating these developmental aspects of S100BB provides essential insights into neurogenesis and brain architecture.
Implications in Neurological Disorders:
Research has indicated potential links between abnormal S100BB levels and neurological disorders. Elevated S100BB levels have been observed in conditions such as traumatic brain injury, stroke, and neurodegenerative diseases. Its release into the bloodstream following CNS damage has positioned S100BB as a biomarker for CNS injury. Additionally, studies have explored its involvement in neuroinflammation and synaptic dysfunction, offering a glimpse into its role in diseases like Alzheimer’s and Parkinson’s.
Conclusion:
S100BB, once regarded as a brain-specific protein, has emerged as a pivotal player in neurological signaling and development. Its intricate involvement in cellular processes within the CNS underscores its significance in understanding brain function and disorders. As research delves deeper into the regulatory mechanisms and functional implications of S100BB, it holds promise for unveiling novel therapeutic targets for neurological diseases. This study aims to shed light on the multifaceted nature of S100BB, emphasizing its crucial roles in the intricate landscape of the central nervous system.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
MORC3 HumanDescription:
MORC Family CW-Type Zinc Finger 3 Human Recombinant
MORC family CW-type zinc finger protein 3, Nuclear matrix protein 2, Zinc finger CW-type coiled-coil domain protein 3, MORC3, KIAA0136, NXP2, ZCWCC3.
Product # :
PRO-2674Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Human MORC Family CW-Type Zinc Finger 3 produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 122kDa. MORC3 is expressed with a 10xHis tag and purified by proprietary chromatographic techniques.
Source
Sf9 insect cells.
Formulation
MORC3 is supplied in 20mM Sodium phosphate, pH 7.6, 500mM NaCl and 20% glycerol.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
MORC Family CW-Type Zinc Finger 3 (MORC3) localizes to the nuclear matrix. MORC3 takes part in the regulation of the tumor suppressor protein p53. MORC3may indicate on dermatomyositis (DM) as autoantibodies against this protein have been found in patients.
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Synonyms
MORC family CW-type zinc finger protein 3, Nuclear matrix protein 2, Zinc finger CW-type coiled-coil domain protein 3, MORC3, KIAA0136, NXP2, ZCWCC3.
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Physical Appearance
Sterile Filtered clear solution.
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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.
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Immunological Functions
1. Binds IgG-type human auto-antibodies.2. immunodot test with positive/negative samples.
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Applications
Western blot with patient sample.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
HBsAg adwDescription:
Hepatitis B Surface Antigen, adw Recombinant
Product # :
HBS-872Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
HbsAg adw produced Pichia Pastoris, having a molecular weight of approximately 24.0 kDa as shown on SDS-PAGE.
Source
Pichia Pastoris.
Formulation
Sterile Filtered solution containing 20mM Phosphate Buffer, 154mM sodium chloride, pH 7.1.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
HBsAg is the surface antigenof the Hepatitis-B-Virus (HBV). The capsidof a virus has different surface proteins from the rest of the virus. The antigen is a protein that binds specifically on one of these surface proteins. It is commonly referred to as the Australian Antigen.
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Physical Appearance
Sterile Filtered pale solution.
-
Stability
HBsAg Should be stored at 4°C.DO NOT FREEZE.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
PTH (7-84) N15 HumanDescription:
Parathyroid Hormone (7-84) N15 Labeled Human Recombinant
Parathyrin, PTH, Parathormone.
Product # :
HOR-013Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
PTH (7-84) N15 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 78 amino acids and having a molecular mass of 8900 Dalton labeled by the stable isotope N15.The PTH (7-84) N15 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PTH (7-84) N15 protein was lyophilized from a 0.2µm filtered concentrated solution in 1xPBS, pH 7.4.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
Parathyroid hormone (PTH), or parathormone, is secreted by the parathyroid glands as a polypeptide containing 84 amino acids. It acts to increase the concentration of calcium in the blood, whereas calcitonin (a hormone produced by the parafollicular cells of the thyroid gland) acts to decrease calcium concentration. PTH acts to increase the concentration of calcium in the blood by acting upon parathyroid hormone receptor in three parts of the body: In the bones- It enhances the release of calcium from the large reservoir contained in the bones. Bone resorption is the normal destruction of bone by osteoclasts, which are indirectly stimulated by PTH. Stimulation is indirect since osteoclasts do not have a receptor for PTH; rather, PTH binds to osteoblasts, the cells responsible for creating bone. Binding stimulates osteoblasts to increase their expression of RANKL, which can bind to osteoclast precursors containing RANK, a receptor for RANKL. The binding of RANKL to RANK stimulates these precursors to fuse, forming new osteoclasts which ultimately enhances the resorption of bone. In the kidney- It enhances active reabsorption of calcium from distal tubules and the thick ascending limb. In the intestine- It enhances the absorption of calcium in the intestine by increasing the production of vitamin D and upregulating the enzyme responsible for 1-alpha hydroxylation of 25-hydroxy vitamin D, converting vitamin D to its active form (1,25-dihydroxy vitamin D) which effects the actual absorption of calcium (as Ca2+ ions) by the intestine via calbindin.
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Synonyms
Parathyrin, PTH, Parathormone.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized PTH (7-84) N15 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution PTH (7-84) N15 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.
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Solubility
It is recommended to reconstitute the lyophilized PTH (7-84) N15 in sterile water not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
LMHNLGKHLN SMERVEWLRK KLQDVHNFVA LGAPLAPRDA GSQRPRKKED NVLVESHEKS LGEADKADVN VLTKAKSQ
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.
- View Data Sheet
Name :
GlycininDescription:
Allergen Ara h 3.0101 Recombinant
Glycinin, Arah3.
Product # :
ALR-008Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Glycinin produced in E. coli is a non- glycosylated, polypeptide chain having a calculated molecular mass of 63 kDa. Glycinin is expressed with a 10xHis tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Glycinin is supplied in 20mM HEPES buffer pH-8, 6M Urea and 0.25M NaCl.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Glycinin Ara h 3 is a seed storage protein, 11 S globulin and trypsin inhibitor from peanut. Each subunit of the hexamer is composed of an acidic and a basic chain derived from a single precursor and linked by a disulfide bond. Ara h 3 and Ara h 4 are isoforms. Glycinin is the source of sulfur-containing amino acids in seed meals and it exists in the seeds of many leguminous and non-leguminous plants.
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Synonyms
Glycinin, Arah3.
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Physical Appearance
Sterile Filtered clear solution.
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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.
-
Immunological Functions
1. Binds IgE type human antibodies. 2. Immunodot test with positive/negative sera panels.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
MumpsDescription:
Mumps Virus Nucleoprotein Recombinant
Product # :
MMP-001Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Full length mumps viral nucleoprotein was expressed from E. coli, the recombinant protein was purified by affinity chromatography technique. The expressed recombinant mumps viral nucleoprotein contains 553 amino acids and a 6 x histidine tag was fused at its N-terminus, having a total Mw of 62kDa.
Source
Escherichia Coli.
Formulation
Phosphate buffer, pH 7.4.
Purity
Protein is >95% pure as determined by 12% PAGE (coomassie staining).
More Info
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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.
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Name :
DNAJC15 HumanDescription:
DnaJ (Hsp40) Homolog, Subfamily C, Member 15 Human Recombinant
DnaJ homolog subfamily C member 15, Cell growth-inhibiting gene 22 protein, Methylation-controlled J protein, MCJ, DNAJC15, DNAJD1, GIG22, HSD18.
Product # :
HSP-057Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
DNAJC15 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 116 amino acids (58-150 a.a.) and having a molecular mass of 12.8 kDa.DNAJC15 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The DNAJC15 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
DNAJC15 which is expressed ubiquitously and located on the membrane contains 1 J domain. In many advanced cases of ovarian adenocarcinoma DNAJC15 is absent or down-regulated, due to hypermethylation and allelic loss. Loss of expression correlates with increased resistance to antineoplastic drugs, such as cisplatin. DNAJC15is a crucial component of the TIM23 translocase complex and stimulates the ATPase activity of HSPA9.
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Synonyms
DnaJ homolog subfamily C member 15, Cell growth-inhibiting gene 22 protein, Methylation-controlled J protein, MCJ, DNAJC15, DNAJD1, GIG22, HSD18.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSFRIWKPL EQVITETAKK ISTPSFSSYY KGGFEQKMSR REAGLILGVS PSAGKAKIRT AHRRVMILNH PDKGGSPYVA AKINEAKDLL ETTTKH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
NNMT MouseDescription:
Nicotinamide N-Methyltransferase Mouse Recombinant
Nicotinamide N-methyltransferase , Nnmt, icotinamide N-methyltransferase isoform1.
Product # :
ENZ-1037Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
NNMT Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 288 amino acids (1-264a.a) and having a molecular mass of 32.1kDa.NNMT is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
NNMT protein solution (1mg/ml) containing 20mM Tris-HCl (pH8.0), 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
NNMT is part of the family of transferases, especially those transferring one-carbon group methyltransferases. NNMT is mostly expressed in the liver, and a lower expression is seen in the kidney, lung, skeletal muscle, placenta and heart. NNMT catalyzes the N-methylation of nicotinamide and other pyridines to form pyridinium ions. This activity is significant for biotransformation of many drugs and xenobiotic compounds. NNMT is accountable for the enzymatic activity which uses S-adenosyl methionine as the methyl donor. NNMT expression is related with tumor stage and DFS time in hepatocellular carcinoma cases. NNMT is a good candidate as a tumor marker of various kinds of cancers. NNMT serum levels have significance in the premature detection and in the management of patients with colorectal cancer.
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Synonyms
Nicotinamide N-methyltransferase , Nnmt, icotinamide N-methyltransferase isoform1.
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Physical Appearance
Sterile filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMESGFT SKDTYLSHFN PRDYLEKYYS FGSRHCAENE ILRHLLKNLF KIFCLGAVKG ELLIDIGSGP TIYQLLSACE SFTEIIVSDY TDQNLWELQK WLKKEPGAFD WSPVVTYVCD LEGNRMKGPE KEEKLRRAIK QVLKCDVTQS QPLGGVSLPP ADCLLSTLCL DAACPDLPAY RTALRNLGSL LKPGGFLVMV DALKSSYYMI GEQKFSSLPL GWETVRDAVE EAGYTIEQFE VISQNYSSTT SNNEGLFSLV GRKPGRSE.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
EFNB2 MouseDescription:
Ephrin- B2 Mouse Recombinant
Ephrin-B2, ELF-2, EPH-related receptor tyrosine kinase ligand 5, LERK-5, HTK ligand, HTK-L, Elf2, Eplg5, Htkl, Lerk5, Efnb2, ELF-2, Epl5, Eplg5, Htk-L, Lerk5, NLERK-1, EFNB2.
Product # :
PRO-2246Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
EFNB2 Mouse Recombinant produced in Sf9 Baculovirus cells is a single polypeptide chain containing 212 amino acids (29-232) and having a molecular mass of 23.4kDa.(Molecular size on SDS-PAGE will appear at approximately 28-40KDa).EFNB2 is fused to 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The EFNB2 solution (0.5mg/1ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Ephrin-B2 belongs to the ephrin (EPH) family. The ephrins and EPH-related receptors contain the largest subfamily of receptor protein-tyrosine kinases and have been associated with mediating developmental events, particularly in the nervous system and in erythropoiesis. Based upon their structures and sequence relationships, ephrins are allocated into the ephrin-A (EFNA) class, which are anchored to the membrane by a glycosylphosphatidylinositol linkage, and the ephrin-B (EFNB) class, which are transmembrane proteins. Ephrin-B2 binds to the EPHB4 and EPHA3 receptors.
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Synonyms
Ephrin-B2, ELF-2, EPH-related receptor tyrosine kinase ligand 5, LERK-5, HTK ligand, HTK-L, Elf2, Eplg5, Htkl, Lerk5, Efnb2, ELF-2, Epl5, Eplg5, Htk-L, Lerk5, NLERK-1, EFNB2.
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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.
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Amino Acid Sequence
RSIVLEPIYW NSSNSKFLPG QGLVLYPQIG DKLDIICPKV DSKTVGQYEY YKVYMVDKDQ ADRCTIKKEN TPLLNCARPD QDVKFTIKFQ EFSPNLWGLE FQKNKDYYII STSNGSLEGL DNQEGGVCQT RAMKILMKVG QDASSAGSAR NHGPTRRPEL EAGTNGRSST TSPFVKPNPG SSTDGNSAGH SGNNLLGSEV ALFALEHHHH HH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
NRG1 HumanDescription:
Heregulin-B2 Human Recombinant
Neuregulin-1, NRG1, GGF, HGL, HRGA, NDF, SMDF, HRG, ARIA, GGF2, HRG1.
Product # :
CYT-407Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Recombinant Human Neuregulin-1 beta 2 produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 61 amino acids and having a total molecular mass of 7.0kDa. NRG-1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered solution in PBS, pH 7.4.
Purity
Greater than 96.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by a cell proliferation assay using serum free human MCF-7 cells is less than 5ng/ml, corresponding to a specific activity of > 2.0 × 105 U/mg.
More Info
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Introduction
Neuregulin is a signaling protein for ErbB2/ErbB4 receptor heterodimers on the cardiac muscle cells, playing an important role in heart structure and function through inducing ErbB2/ErbB4 receptor phosphorylation and cardiomyocyte differentiation. Research on molecular level discovered that neuregulin recombinant could make disturbed myocardial cell structure into order and strengthen the connection between myocardial cells by intercalated discs re-organization. Pharmacodynamic experiments in animals showed that neuregulin (NRG1) recombinant can reduce the degree of damage on myocardial cells caused by ischemia, hypoxia and viral infection.
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Synonyms
Neuregulin-1, NRG1, GGF, HGL, HRGA, NDF, SMDF, HRG, ARIA, GGF2, HRG1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized NRG1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Heregulin 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 NRG1 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
SHLVKCAEKEKTFCVNGGECFMVKDLSNPSRYLCKCPNEFTGDRCQNYVMASFYKAEELYQ.
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.
- View Data Sheet
Name :
NEFL BovineDescription:
Neurofilament Light Bovine
Neurofilament light polypeptide, NF-L, NEFL, NF68, NFL, 68 kDa neurofilament protein.
Product # :
PRO-2786Price :
Quantity :
Shipping Method :
Shipped at Room temp
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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
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Synonyms
Neurofilament light polypeptide, NF-L, NEFL, NF68, NFL, 68 kDa neurofilament protein.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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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.
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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.
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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.