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1000 results found for “ectodysplasin”
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Name :
TDP1 HumanDescription:
Tyrosyl-DNA Phosphodiesterase 1 Human Recombinant
Tyrosyl-DNA phosphodiesterase 1, TDP1 protein, TDP1.
Product # :
ENZ-685Price :
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Description
TDP1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 318 amino acids (1-298) and having a molecular mass of 35.8kDa. TDP1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The TDP1 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
Tyrosyl-DNA phosphodiesterase 1 ( TDP1) is required for repairing stalled topoisomerase I-DNA complexes by catalyzing the hydrolysis of the phosphodiester bond between the tyrosine residue of topoisomerase I and the 3-prime phosphate of DNA. TDP1 also detach glycolate from single-stranded DNA having 3-prime phosphoglycolate, suggesting a role in repair of free-radical mediated DNA double-strand breaks.
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Synonyms
Tyrosyl-DNA phosphodiesterase 1, TDP1 protein, TDP1.
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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 MSQEGDYGRW TISSSDESEE EKPKPDKPST SSLLCARQGA ANEPRYTCSE AQKAAHKRKI SPVKFSNTDS VLPPKRQKSG SQEDLGWCLS SSDDELQPEM PQKQAEKVVI KKEKDISAPN DGTAQRTENH GAPACHRLKE EEDEYETSGE GQDIWDMLDK GNPFQFYLTR VSGVKPKYNS GALHIKDILS PLFGTLVSSA QFNYCFDVDW LVKQYPPEFR KKPILLVHGD KREAKAHLHA QAKPYENISL CQAKLDIAFG THHTKMMLLL YEEGLRVVIH TSNLIHADWH QKTQGTHL.
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 :
GID8 HumanDescription:
GID Complex Subunit 8 Human Recombinant
GID Complex Subunit 8, C20orf11, TWA1, Two Hybrid-Associated Protein 1 With RanBPM,GID Complex Subunit 8 Homolog (S. Cerevisiae), Glucose-Induced Degradation Protein 8 Homolog, Chromosome 20 Open Reading Frame 11, GID Complex Subunit 8 Homolog, Protein C20orf11, GID8.
Product # :
PRO-2191Price :
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Description
GID8 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 251 amino acids (1-228 a.a) and having a molecular mass of 29.1kDa.GID8 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GID8 protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4), 20% glycerol and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
GID Complex Subunit 8, also known as GID8 is a member of the GID8 family. GID8 was recognized through a two hybrid-associated protein screen with RanBPM. GID8 acts together with RanBP9 and includes a protein complex with RanBPM and Muskelin.
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Synonyms
GID Complex Subunit 8, C20orf11, TWA1, Two Hybrid-Associated Protein 1 With RanBPM,GID Complex Subunit 8 Homolog (S. Cerevisiae), Glucose-Induced Degradation Protein 8 Homolog, Chromosome 20 Open Reading Frame 11, GID Complex Subunit 8 Homolog, Protein C20orf11, GID8.
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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 MGSMSYAEKP DEITKDEWME KLNNLHVQRA DMNRLIMNYL VTEGFKEAAE KFRMESGIEP SVDLETLDER IKIREMILKG QIQEAIALIN SLHPELLDTN RYLYFHLQQQ HLIELIRQRE TEAALEFAQT QLAEQGEESR ECLTEMERTL ALLAFDSPEE SPFGDLLHTM QRQKVWSEVN QAVLDYENRE STPKLAKLLK LLLWAQNELD QKKVKYPKMT DLSKGVIEEP K
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 :
PRKAR1ADescription:
cAMP-Dependent Protein Kinase A regulatory subunit I a Recombinant
cAMP-dependent protein kinase type I-alpha regulatory subunit, Tissue-specific extinguisher 1, TSE1, CAR, CNC, CNC1, PKR1, PPNAD1, PRKAR1, PRKAR1A, MGC17251, DKFZp779L0468.
Product # :
PKA-201Price :
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Description
cAMP-dependent PKA is an ubiquitous serine/theonine protein kinase present in a variety of tissues (e.g. brain, skeletal muscle, heart). The intracellular cAMP level regulates cellular responses by altering the interaction between the catatytic C and regulatory R subunits of PKA. The inactive tetrameric PKA holoenzyme R2C2 is activated when cAMP binds to R2, which dissociates the tetramer to R2 cAMP 4 and two active catalytic subunits. Free Catalytic subunits of PKA can phosphorylate a wide variety of intracellular target proteins. In response to hormone- induced high cAMP levels, PKA phosphorylates glycogen synthetase (inhibition of the enzyme activity) and phosphorylase kinase to block glycogen synthesis. Different isoforms of catalytic and regulatory subunits suggest specific functions. The recombinant PKA regulatory subunit I a is a dimeric 90kDa protein.
Source
Escherichia Coli.
Formulation
PKA regulatory subunit I a is supplied in 50% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Synonyms
cAMP-dependent protein kinase type I-alpha regulatory subunit, Tissue-specific extinguisher 1, TSE1, CAR, CNC, CNC1, PKR1, PPNAD1, PRKAR1, PRKAR1A, MGC17251, DKFZp779L0468.
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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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Unit Definition
Specifically inhibits PKA catalytic subunit (Ki about 0.1nM). Activity can be restored by adding cAMP (Kact about 100nM). The binding of the catalytic subunit is dependent on the presence of ATP and Mg.
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 :
Vaspin Human, HisDescription:
Vaspin Human Recombinant, His Tag
Serpin A12 precursor, Visceral adipose-specific serpin, Visceral adipose tissue- derived serine protease inhibitor, Vaspin, OL-64, SERPINA12, Serine (or cysteine) proteinase inhibitor, clade A, antitrypsin, alpha-1 antiproteinase.
Product # :
CYT-459Price :
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Description
Vaspin Human Recombinant produced in E.Coli is a single, non-glycosylated, His Tag, polypeptide chain containing 415 amino acids and having a molecular mass of 47 kDa.The Vaspin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Vaspin in 20mM Tris pH-8, 0.2mM PMSF and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Vaspin (visceral adipose-specific SERPIN), a newly identified adipokine, which is a member of serine protease inhibitor family. Vaspin is also a unique insulin sensitizing adipocytokine in obesity. A recent publication indicates that induction of human vaspin mRNA expression in adipose tissue is regulated in a fat depot-specific manner and could be associated with parameters of obesity, insulin resistance, and glucose metabolism.
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Synonyms
Serpin A12 precursor, Visceral adipose-specific serpin, Visceral adipose tissue- derived serine protease inhibitor, Vaspin, OL-64, SERPINA12, Serine (or cysteine) proteinase inhibitor, clade A, antitrypsin, alpha-1 antiproteinase.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Liquid Vaspin although stable at 10°C for 1 week, should be stored 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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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MLKPSFSPRN YKALSEVQGW KQRMAAKELA RQNMDLGFKL LKKLAFYNPG RNIFLSPLSI STAFSMLCLG AQDSTLDEIK QGFNFRKMPE KDLHEGFHYI IHELTQKTQD LKLSIGNTLF IDQRLQPQRK FLEDAKNFYS AETILTNFQN LEMAQKQIND FISQKTHGKI NNLIENIDPG TVMLLANYIF FRARWKHEFD PNVTKEEDFF LEKNSSVKVP MMFRSGIYQV GYDDKLSCTI LEIPYQKNIT AIFILPDEGK LKHLEKGLQV DTFSRWKTLL SRRVVDVSVP RLHMTGTFDL KKTLSYIGVS KIFEEHGDLT KIAPHRSLKV GEAVHKAELK MDERGTEGAA GTGAQTLPME TPLVVKIDKP YLLLIYSEKI PSVLFLGKIV NPIGK.
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 :
CCL22 Human, HisDescription:
Macrophage-Derived Chemokine Human Recombinant (CCL22), His Tag
C-C motif chemokine 22, Small-inducible cytokine A22, Macrophage-derived chemokine, MDC(1-69), Stimulated T-cell chemotactic protein 1, CC chemokine STCP-1, CCL22, MDC, SCYA22, ABCD-1, DC/B-CK, MGC34554, A-152E5.1.
Product # :
CHM-367Price :
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Description
MDC Human Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 90 amino acids (25-93 a.a.) and having a molecular mass of 10.3 kDa. The MDC is fused to 21 amino acid His-Tag at N-terminus purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The MDC protein contains phosphate-buffered Saline (PBS) pH7.4 and 10% glycerol.
Purity
Greater than 95% as determined by Analysis by SDS-PAGE.
SDS-PAGE
More Info
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Introduction
MDC (CCL22) is a small cytokine that belongs to the CC chemokine family. CCL22 is one of several Cys-Cys (CC) cytokine genes clustered on the q arm of chromosome 16. MDC shows chemotactic activity for natural killer cells, chronically activated T lymphocytes, monocytes and dendritic cells. On the other hand, MDC shows a mild activity for primary activated T lymphocytes and has no chemoattractant activity for neutrophils, eosinophils and resting T lymphocytes. MDC may also have a role in the trafficking of activated T lymphocytes to inflammatory sites and other aspects of activated T lymphocyte physiology. MDC interacts with cell surface chemokine receptors CCR4.
CCL22 is vastly expressed in macrophage and in monocyte-derived dendritic cells, and thymus. CCL22 is also found in the lymph node, appendix, activated monocytes, resting and activated macrophages. Lower expression of CCL22 can be seen in the lung and the spleen and very weak expression in the small intestine. In the lymph node CCL22 is expressed in a mature subset of Langerhans' cells (CD1a+ and CD83+).
Furthermore, CCL22 is expressed in atopic dermatitis, allergic contact dermatitis skin, and psoriasis, in both the epidermis and dermis. In addition, MDC has a role in hindering progression of lung cancer. Moreover, significantly higher CCL22 expression is linked to gastric cancer. -
Synonyms
C-C motif chemokine 22, Small-inducible cytokine A22, Macrophage-derived chemokine, MDC(1-69), Stimulated T-cell chemotactic protein 1, CC chemokine STCP-1, CCL22, MDC, SCYA22, ABCD-1, DC/B-CK, MGC34554, A-152E5.1.
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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
MGSSHHHHHH SSGLVPRGSH MGPYGANMED SVCCRDYVRY RLPLRVVKHF YWTSDSCPRP GVVLLTFRDK EICADPRVPW VKMILNKLSQ.
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Background
What is the molecular weight/Mw of CCL22 HUMAN, HIS Protein?
CCL22 HUMAN, HIS Protein has a total Mw of 10.3kDa.
What is the source or expression system of CCL22 HUMAN, HIS Protein?
Escherichia Coli.
What is the Purity of CCL22 HUMAN, HIS Protein?
CCL22 HUMAN, HIS Protein is > 95% pure as determined by SDS-PAGE.
What is the Biological Activity of CCL22 HUMAN, HIS Protein?
The biological functionality of CCL22 HUMAN, HIS Protein will be determined in the future.
What is the amino acid sequence of CCL22 HUMAN, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MGPYGANMED SVCCRDYVRY RLPLRVVKHF YWTSDSCPRP GVVLLTFRDK EICADPRVPW VKMILNKLSQ
What applications can CCL22 HUMAN, HIS Protein be used in?
CCL22 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CCL22 HUMAN, HIS Protein?
The endotoxin level is minimal, CCL22 HUMAN, HIS 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.
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Name :
MINA HumanDescription:
MYC Induced Nuclear Antigen Human Recombinant
MYC Induced Nuclear Antigen, MINA53, MDIG, 60S Ribosomal Protein L27a Histidine Hydroxylase, Mineral Dust-Induced Gene Protein, Histone Lysine Demethylase MINA Ribosomal Oxygenase MINA, Nucleolar Protein 52, NO52, ROX, Bifunctional Lysine-Specific Demethylase And Histidyl-Hydroxylase MINA, Myc-Induced Nuclear Antigen, 53 KDa, Mineral Dust Induced Gene Protein, MYC-Induced Nuclear Antigen, EC 1.14.11.-, Bifunctional lysine-specific demethylase and histidyl-hydroxylase MINA.
Product # :
PRO-2078Price :
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Description
MINA Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 485 amino acids (1-465 a.a) and having a molecular mass of 54.9kDa. MINA is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MINA protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
MYC Induced Nuclear Antigen, also known as MINA is an oxygenase which can function both as a histone lysine demethylase and a ribosomal histidine hydroxylase. MINA is involved in the demethylation of trimethylated Lys-9 on histone H3 (H3K9me3), leading to an increase in ribosomal RNA expression. MINA also catalyzes the hydroxylation of 60S ribosomal protein L27a on His-39. In addition, MINA plays a significant role in cell growth and survival. MINA is implicated in ribosome biogenesis, probably in the duration of the assembly process of pre-ribosomal particles.
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Synonyms
MYC Induced Nuclear Antigen, MINA53, MDIG, 60S Ribosomal Protein L27a Histidine Hydroxylase, Mineral Dust-Induced Gene Protein, Histone Lysine Demethylase MINA Ribosomal Oxygenase MINA, Nucleolar Protein 52, NO52, ROX, Bifunctional Lysine-Specific Demethylase And Histidyl-Hydroxylase MINA, Myc-Induced Nuclear Antigen, 53 KDa, Mineral Dust Induced Gene Protein, MYC-Induced Nuclear Antigen, EC 1.14.11.-, Bifunctional lysine-specific demethylase and histidyl-hydroxylase MINA.
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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 MPKKAKPTGS GKEEGPAPCK QMKLEAAGGP SALNFDSPSS LFESLISPIK TETFFKEFWE QKPLLIQRDD PALATYYGSL FKLTDLKSLC SRGMYYGRDV NVCRCVNGKK KVLNKDGKAH FLQLRKDFDQ KRATIQFHQP QRFKDELWRI QEKLECYFGS LVGSNVYITP AGSQGLPPHY DDVEVFILQL EGEKHWRLYH PTVPLAREYS VEAEERIGRP VHEFMLKPGD LLYFPRGTIH QADTPAGLAH STHVTISTYQ NNSWGDFLLD TISGLVFDTA KEDVELRTGI PRQLLLQVES TTVATRRLSG FLRTLADRLE GTKELLSSDM KKDFIMHRLP PYSAGDGAEL STPGGKLPRL DSVVRLQFKD HIVLTVLPDQ DQSDETQEKM VYIYHSLKNS RETHMMGNEE ETEFHGLRFP LSHLDALKQI WNSPAISVKD LKLTTDEEKE SLVLSLWTEC LIQVV.
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 :
SIRPA Human, HEKDescription:
Signal-Regulatory Protein Alpha Human Recombinant, HEK
Tyrosine-protein phosphatase non-receptor type substrate 1 isoform 1, SHP substrate 1, SHPS-1, Brain Iglike molecule with tyrosine-based activation motifs, Bit, CD172 antigen-like family member A, MYD1, PTPNS1, SHPS1,SIRP, Inhibitory receptorSHPS-1, Macrophage fusion receptor, MyD-1 antigen, Signal-regulatory protein alpha-1, Sirp-alpha-1, Signalregulatory protein alpha-2, Sirp-alpha-2, Signal-regulatory protein alpha-3, Sirp-alpha-3, p84, CD172a, BIT, MFR.
Product # :
PRO-2755Price :
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Description
SIRPA Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (27-373a.a) containing 356 amino acids and having a molecular mass of 39kDa.SIRPA is fused to a 6 amino acid His-tag at C-terminus,and is purified by proprietary chromatographic techniques.
Source
HEK293 Cells.
Formulation
The SIRPA solution (1mg/ml) contains Phosphate-Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
Biological Activity
Measured by its binding ability in a functional ELISA with Human CD47.
More Info
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Introduction
Signal-Regulatory Protein Alpha, SIRPA belongs to the signal-regulatory-protein (SIRP) family, as well as the immunoglobulin super family. The members of the SIRP family are receptor-type transmembrane glycoproteins which are involved in the negative regulation of receptor tyrosine kinase-coupled signaling processes.
SIRPA can be phosphorylated by tyrosine kinases. The phospho-tyrosine residues of this PTP have been shown to recruit SH2 domain containing tyrosine phosphatases (PTP), and perform as substrates of PTPs. SIRPA take part in signal transduction mediated by a variety of growth factor receptors. CD47 has been shown to be a ligand for SIRPA. -
Synonyms
Tyrosine-protein phosphatase non-receptor type substrate 1 isoform 1, SHP substrate 1, SHPS-1, Brain Iglike molecule with tyrosine-based activation motifs, Bit, CD172 antigen-like family member A, MYD1, PTPNS1, SHPS1,SIRP, Inhibitory receptor
SHPS-1, Macrophage fusion receptor, MyD-1 antigen, Signal-regulatory protein alpha-1, Sirp-alpha-1, Signalregulatory protein alpha-2, Sirp-alpha-2, Signal-regulatory protein alpha-3, Sirp-alpha-3, p84, CD172a, BIT, MFR. -
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
DGSGVAGEEE LQVIQPDKSV LVAAGETATL RCTATSLIPV GPIQWFRGAG PGRELIYNQK EGHFPRVTTV SDLTKRNNMD FSIRIGNITP ADAGTYYCVK FRKGSPDDVE FKSGAGTELS VRAKPSAPVV SGPAARATPQ HTVSFTCESH GFSPRDITLK WFKNGNELSD FQTNVDPVGE SVSYSIHSTA KVVLTREDVH SQVICEVAHV TLQGDPLRGT ANLSETIRVP PTLEVTQQPV RAENQVNVTC QVRKFYPQRL QLTWLENGNV SRTETASTVT ENKDGTYNWM SWLLVNVSAH RDDVKLTCQV EHDGQPAVSK SHDLKVSAHP KEQGSNTAAE NTGSNERNIY HHHHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
EDN3 HumanDescription:
Endothelin-3 Human Recombinant
EDN3, EDN-3, ET-3, ET3, WS4B, HSCR4, MGC15067, MGC61498, Endothelin-3, Preproendothelin-3, PPET3.
Product # :
HOR-017Price :
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Description
EDN3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 236 amino acids (26-238 a.a) and having a molecular mass of 25.2kDa.EDN3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Formulation
EDN3 protein solution (0.25mg/ml) in Phosphate buffered saline (pH7.4) and 10% glycerol.
Purity
Greater than 85.0% as determined by RP-HPLC.
More Info
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Introduction
EDN3 interacts with endothelin receptor B, on the surface of cells. Throughout embryonic development, EDN3 takes part in neural crest cells that migrate from the developing spinal cord to specific regions in the embryo, where they give rise to many different types of cells. EDN3 and EDN3R are necessary for the formation of nerves in the large intestine (enteric nerves) and melanocytes (produce melanin). Mutations in the EDN3 gene is linked with Waardenburg syndrome, type IV that is characterized by changes in skin, hair, and eye coloring. Mutations in the EDN3 gene is linked with Hirschsprung disease that causes severe constipation or intestinal blockage
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Synonyms
EDN3, EDN-3, ET-3, ET3, WS4B, HSCR4, MGC15067, MGC61498, Endothelin-3, Preproendothelin-3, PPET3.
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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 MGSGDAGRRG VSQAPTAARS EGDCEETVAG PGEETVAGPG EGTVAPTALQ GPSPGSPGQE QAAEGAPEHH RSRRCTCFTY KDKECVYYCH LDIIWINTPE QTVPYGLSNY RGSFRGKRSA GPLPGNLQLS HRPHLRCACV GRYDKACLHF CTQTLDVSSN SRTAEKTDKE EEGKVEVKDQ QSKQALDLHH PKLMPGSGLA LAPSTCPRCL FQEGAP.
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 :
TXNDC12 HumanDescription:
Thioredoxin Domain Containing 12 Human Recombinant
Thioredoxin domain containing 12 (endoplasmic reticulum), Endoplasmic reticulum resident protein 18, Endoplasmic reticulum resident protein 19, endoplasmic reticulum thioredoxin superfamily member 18 kDa, thioredoxin domain-containing protein 12, protein disulfide isomerase family A member 16, endoplasmic reticulum protein ERp19, anterior gradient homolog 1, Thioredoxin-like protein p19, ER protein 18, ERP18, ER protein 19, ERP19, ERP16, TLP19, AGR1, PDIA16, hAG-1, EC 1.8.4.2.
Product # :
PRO-1133Price :
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Description
TXNDC12 Human Recombinant produced in E. coli is a single polypeptide chain containing 184 amino acids (27-172) and having a molecular mass of 20.8 kDa.TXNDC12 is fused to a 38 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The TXNDC12 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
TXNDC12 is a member of the thioredoxin super family. This Family members have a thioredoxin fold with a consensus active-site sequence (CxxC) and take part in redox regulation, protection against oxidative stress, refolding of disulfide-containing proteins, and regulation of transcription factors.
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Synonyms
Thioredoxin domain containing 12 (endoplasmic reticulum), Endoplasmic reticulum resident protein 18, Endoplasmic reticulum resident protein 19, endoplasmic reticulum thioredoxin superfamily member 18 kDa, thioredoxin domain-containing protein 12, protein disulfide isomerase family A member 16, endoplasmic reticulum protein ERp19, anterior gradient homolog 1, Thioredoxin-like protein p19, ER protein 18, ERP18, ER protein 19, ERP19, ERP16, TLP19, AGR1, PDIA16, hAG-1, EC 1.8.4.2.
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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
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMHN GLGKGFGDHI HWRTLEDGKK EAAASGLPLM VIIHKSWCGA CKALKPKFAE STEISELSHN FVMVNLEDEE EPKDEDFSPD GGYIPRILFL DPSGKVHPEI INENGNPSYK YFYVSAEQVV QGMKEAQERL TGDAFRKKHL EDEL
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 :
Y.Enterocolitica (O:9) YopHDescription:
Yersinia Enterocolitica (O:9) YopH Recombinant
Product # :
PRO-2275Price :
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Description
Recombinant Yersinia Enterocolitica (O:9) YopH produced in E.coli is a non-glycosylated, polypeptide chain having a calculated molecular mass of 52,311 Dalton. Y.Enterocolitica (O:9) YopH is expressed with a 10xHis tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Y.Enterocolitica (O:9) YopH is supplied in 20mM HEPES buffer pH-7.6, 250mM NaCl and 20% glycerol.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
Yersinia enterocolitica is a Gram-negative bacillus-shaped bacterium, which is a member of the Enterobacteriaceae family. Y.Enterocolitica is motile at temperatures between 22-29°C, however becomes non-motile at normal human body temperature. Y. Enterocolitica infection causes the yersiniosis disease, which is an animal-borne disease occurring in humans, as well as in a various groups of animals such as cattle, deer, pigs, and birds. Yersinia enterocolitica is a heterogeneous group of strains, which are conventionally classified by bio-typing into six bio-groups on the basis of phenotypic characteristics, and by serotyping into more than 57 “O” serogroups, on the basis of their O (lipopolysaccharide or LPS) surface antigen. Five of the six biogroups (1B and 2–5) are considered as pathogens. Nevertheless, only a few of these serogroups have been linked with disease in either humans or animals. Strains which belong to serogroups O:3 (biogroup 4), O:5,27 (biogroups 2 and 3), O:8 (biogroup 1B), and O:9 (biogroup 2) are most frequently isolated worldwide from human samples. Still, the main Y. enterocolitica serogroup in many European countries is serogroup O:3 followed by O:9, whereas the serogroup O:8 is mostly detected in the United States.
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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- and IgM- and IgA-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.
- View Data Sheet
Name :
sCD23 HumanDescription:
Soluble CD23 Human Recombinant
Low affinity immunoglobulin epsilon Fc receptor, Lymphocyte IgE receptor, Fc-epsilon-RII, BLAST-2, Immunoglobulin E-binding factor, CD23 antigen, FCER2, CD23, FCE2, CD23A, IGEBF, CLEC4J.
Product # :
PRO-1789Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
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Description
sCD23 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 172 amino acids and having a molecular mass of 19.2kDa.The sCD23 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 is determined by its ability to induce TNF-alpha production by human PBMCs.More Info
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Introduction
CD23 is a 45kDa glycoprotein, which is present on a subpopulation of freshly isolated peripheral blood and tonsil B cells and strongly expressed on EBV-transformed B lymphoblasts. The CD23 molecule is identical to the low affinity IgE receptor found on B cells. Expression of CD23 has been detected in neoplastic cells from cases of B cell chronic lymphocyctic leukaemia and some cases of centroblastic/centrocytic lymphoma.
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Synonyms
Low affinity immunoglobulin epsilon Fc receptor, Lymphocyte IgE receptor, Fc-epsilon-RII, BLAST-2, Immunoglobulin E-binding factor, CD23 antigen, FCER2, CD23, FCE2, CD23A, IGEBF, CLEC4J.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized sCD23 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution sCD23 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 sCD23 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MELQVSSGFV CNTCPEKWIN FQRKCYYFGK GTKQWVHARY ACDDMEGQLV SIHSPEEQDF LTKHASHTGS WIGLRNLDLK GEFIWVDGSH VDYSNWAPGE PTSRSQGEDC VMMRGSGRWN DAFCDRKLGA WVCDRLATCT PPASEGSAES MGPDSRPDPD GRLPTPSAPL HS
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 :
I TAC HumanDescription:
I-TAC Human Recombinant (CXCL11)
Small inducible cytokine B11, CXCL11, I-TAC, IP-9, H174, Beta-R1, chemokine (C-X-C motif) ligand 11, IP9, b-R1, SCYB11, SCYB9B, MGC102770.
Product # :
CHM-334Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
I-TAC Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 73 amino acids and having a molecular mass of 8300 Dalton. The I-TAC is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2?m filtered concentrated (0.5mg/ml) solution in 20mM PB, pH 7.4, 100mM NaCl.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Determined by its ability to chemoattract human IL-2 activated T-Lymphocytes using a concentration range of 0.1-10.0 ng/ml.More Info
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Introduction
Chemokine (C-X-C motif) ligand 11 (CXCL11) is a small cytokine belonging to the CXC chemokinen family that is also called inducible T-cell alpha chemoattractant (I-TAC) and (IP-9). I-TAC is highly expressed in peripheral blood leukocytes, pancreas and liver, with moderate levels in thymus, spleen and lung and low expression levels were in small intestine, placenta and prostate. Gene expression of CXCL11 is strongly induced by IFN-g and IFN-b, and weakly induced by IFN-a. The I-TAC chemokine elicits its effects on its target cells by interacting with the cell surface chemokine receptor CXCR3, with a higher affinity than do the other ligands for this receptor, CXCL9 and CXCL10. I-TAC is chemotactic for activated T cells. The CXCL11 gene is located on human chromosome 4 along with many other members of the CXC chemokine family.
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Synonyms
Small inducible cytokine B11, CXCL11, I-TAC, IP-9, H174, Beta-R1, chemokine (C-X-C motif) ligand 11, IP9, b-R1, SCYB11, SCYB9B, MGC102770.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized I-TAC although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution I-TAC 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 I-TAC 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
FPMFKRGRCLCIGPGVKAVKVADIEKASIMYPSNNCDKIEVIITLKENKGQRCLNPKSKQARLIIKKVERKNF.
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 :
TECK MouseDescription:
Thymus Expressed Chemokine Mouse Recombinant (CCL25)
C-C motif chemokine 25, Small-inducible cytokine A25, Thymus-expressed chemokine, Chemokine TECK, CCL25, SCYA25, TECK, Ckb15, MGC150327.
Product # :
CHM-259Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
TECK Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 121 amino acids and having a molecular mass of 14.1kDa. The TECK is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Filtered (0.2µm) and lyophilized from a concentrated (1mg/ml) solution in in 1×PBS, pH7.4.
Purity
Greater than 97.0% as determined by
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Determined by its ability to chemoattract human CCR9 transfected BaF3 mouse pro-B cells using a concentration range of 0.1-0.5 ug/ml.More Info
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Introduction
CCL25 (Teck) is a novel CC chemokine, which is distantly related (about 20% amino acid sequence identity) to other CC chemokines. The mouse CCL25 cDNA has also been cloned and shown to encode a 144 a.a. protein, which exhibits 49% a.a. sequence identity to the human CCL25. Human and mouse CCL25 expression was shown to be greatly restricted to the thymus and small intestine. While dendritic cells are identified as the source of CCL25 production in the thymus, dendritic cells derived from bone marrow do not express CCL25. CCL25 signals through the CCR9 receptor. Teck is possibly involved in T-cell development.
Recombinant human and mouse Teck were shown to be chemotactic for activated macrophages, dendritic cells and thymocytes. The recombinant protein demonstrates chemotactic activity on thymocytes, macrophages, THP-1 cells, and dendritic cells but is inactive on peripheral blood lymphocytes and neutrophils. -
Synonyms
C-C motif chemokine 25, Small-inducible cytokine A25, Thymus-expressed chemokine, Chemokine TECK, CCL25, SCYA25, TECK, Ckb15, MGC150327.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized TECK although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TECK 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 TECK in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
QGAFEDCCLG YQHRIKWNVL RHARNYHQQE VSGSCNLRAV RFYFRQKVVC GNPEDMNVKR AIRILTARKR LVHWKSASDS QTERKKSNHM KSKVENPNST SVRSATLGHP RMVMMPRKTN N
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 :
Lymphotactin HumanDescription:
Lymphotactin Human Recombinant (XCL1)
XCL1, Cytokine SCM-1, ATAC, Lymphotaxin, SCM-1-alpha, Small inducible cytokine C1, XC chemokine ligand 1, LTN, LPTN, SCM1, SCM-1, SCYC1, SCM-1a.
Product # :
CHM-314Price :
Quantity :
Shipping Method :
Shipped at Room temp
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- source
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Description
Lymphotactin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 92 amino acids and having a molecular mass of 10007 Dalton. The Lymphotactin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The XCL1 was lyophilized from a concentrated (1mg/ml) solution in water containing no additives.
Purity
Greater than 99.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The Biological activity is calculated by its ability to chemoattract human T cells at 10-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.More Info
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Introduction
Chemokine (C motif) ligand (XCL1) is a small cytokine belonging to the XC chemokine family that is also known as lymphotactin. It is found in high levels in spleen, thymus, intestine and peripheral blood leukocytes, and at lower levels in lung, prostate gland and ovary. Cellular sources for XCL1 include activated thymic and peripheral blood CD8+ T cells. This chemokine attracts T cells. In humans, XCL1 is closely related to another chemokine called XCL2, whose geneis found at the same locus on chromosome 1. XCL1 induces it chemotactic function by binding to a chemokine receptor called XCR1.
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Synonyms
XCL1, Cytokine SCM-1, ATAC, Lymphotaxin, SCM-1-alpha, Small inducible cytokine C1, XC chemokine ligand 1, LTN, LPTN, SCM1, SCM-1, SCYC1, SCM-1a.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Lymphotactin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution XCL1 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 avoid freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Lymphotactin 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
The sequence of the first five N-terminal amino acids was determined and was found to be Gln-Ser-Glu-Val-Ser.
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 :
PSPN MouseDescription:
Persephin Mouse Recombinant
Persephin, PSPN.
Product # :
CYT-802Price :
Quantity :
Shipping Method :
Shipped at Room temp
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- source
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Description
PSPN Mouse Recombinant produced in E.Coli is a disulfide-linked homodimer containing 2x96 amino acids and having a molecular mass of 20.7kDa. The PSPN is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2?m filtered concentrated solution in 30 %ACN, 0.1 %TFA, 150mM NaCl.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Fully biologically active when compared to standard. The ED50 as determined by a cell proliferation assay using human TT medullary thyroid cancer cells is less than 0.1ng/ml, corresponding to a specific activity of > 1.0 × 10,000,000 IU/mg.More Info
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Introduction
Persephin is a member of the GDNF ligand subfamily of the TGF-beta superfamily. PSPN encourages the existence and growth of key dopaminergic and motor neurons, as well as taking part in kidney development. Nonetheless, persephin does not support existence of peripheral neurons.
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Synonyms
Persephin, PSPN.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized PSPN although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution PSPN 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 PSPN 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
ALAGSCRLWS LTLPVAELGL GYASEEKVIF RYCAGSCPQE ARTQHSLVLA RLRGRGRAHG RPCCQPTSYA DVTFLDDQHH WQQLPQLSAA ACGCGG
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 :
SIRPA HumanDescription:
Signal-Regulatory Protein Alpha Human Recombinant
Signal-Regulatory Protein Alpha, SHPS1, CD172 Antigen-Like Family Member A, Inhibitory Receptor SHPS-1, Macrophage Fusion Receptor, PTPNS1, SIRP, P84, BIT, MFR, Brain-Immunoglobulin-Like Molecule With Tyrosine-Based Activation Motifs, Brain Ig-Like Molecule With Tyrosine-Based Activation Motifs, Protein Tyrosine Phosphatase, Non-Receptor Type Substrate 1, Tyrosine-Protein Phosphatase Non-Receptor Type Substrate 1, Tyrosine Phosphatase SHP Substrate 1, Signal-Regulatory Protein Alpha-1 , ignal-Regulatory Protein Alpha-2, Signal-Regulatory Protein Alpha-3, SHP Substrate 1, CD172a Antigen, Myd-1 Antigen, MyD-1 Antigen, Sirp-Alpha-1, Sirp-Alpha-2, Sirp-Alpha-3, CD172A, SHPS-1, MYD-1, MYD1, Tyrosine-protein phosphatase non-receptor type substrate 1.
Product # :
PRO-2080Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SIRPA Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 370 amino acids (27-373 a.a) and having a molecular mass of 40.4kDa. SIRPA is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
SIRPA protein solution (0.5mg/ml) containing PBS buffer (pH 7.4), 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Signal-Regulatory Protein Alpha, SIRPA belongs to the signal-regulatory-protein (SIRP) family, as well as theimmunoglobulin super family. The members of the SIRP family are receptor-type transmembrane glycoproteins which areinvolved in the negative regulation of receptor tyrosine kinase-coupled signaling processes. SIRPA can bephosphorylated by tyrosine kinases. The phospho-tyrosine residues of this PTP have been shown to recruit SH2domain containing tyrosine phosphatases (PTP), and perform as substrates of PTPs. SIRPA take part insignal transduction mediated by a variety of growth factor receptors. CD47 has been shown to be a ligand for SIRPA.
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Synonyms
Signal-Regulatory Protein Alpha, SHPS1, CD172 Antigen-Like Family Member A, Inhibitory Receptor SHPS-1, Macrophage Fusion Receptor, PTPNS1, SIRP, P84, BIT, MFR, Brain-Immunoglobulin-Like Molecule With Tyrosine-Based Activation Motifs, Brain Ig-Like Molecule With Tyrosine-Based Activation Motifs, Protein Tyrosine Phosphatase, Non-Receptor Type Substrate 1, Tyrosine-Protein Phosphatase Non-Receptor Type Substrate 1, Tyrosine Phosphatase SHP Substrate 1, Signal-Regulatory Protein Alpha-1 , ignal-Regulatory Protein Alpha-2, Signal-Regulatory Protein Alpha-3, SHP Substrate 1, CD172a Antigen, Myd-1 Antigen, MyD-1 Antigen, Sirp-Alpha-1, Sirp-Alpha-2, Sirp-Alpha-3, CD172A, SHPS-1, MYD-1, MYD1, Tyrosine-protein phosphatase non-receptor type substrate 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
MGSSHHHHHH SSGLVPRGSH MGSGVAGEEE LQVIQPDKSV LVAAGETATL RCTATSLIPV GPIQWFRGAG PGRELIYNQK EGHFPRVTTV SDLTKRNNMD FSIRIGNITP ADAGTYYCVK FRKGSPDDVE FKSGAGTELS VRAKPSAPVV SGPAARATPQ HTVSFTCESH GFSPRDITLK WFKNGNELSD FQTNVDPVGE SVSYSIHSTA KVVLTREDVH SQVICEVAHV TLQGDPLRGT ANLSETIRVP PTLEVTQQPV RAENQVNVTC QVRKFYPQRL QLTWLENGNV SRTETASTVT ENKDGTYNWM SWLLVNVSAH RDDVKLTCQV EHDGQPAVSK SHDLKVSAHP KEQGSNTAAE NTGSNERNIY.
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 :
EBI3 HumanDescription:
Epstein Barr Virus Induced 3 Human Recombinant
Interleukin-27 subunit beta, IL-27 subunit beta, IL-27B, Epstein-Barr virus-induced gene 3 protein, EBV-induced gene 3 protein, EBI3, IL27B.
Product # :
CYT-367Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
EBI3 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 209 amino acids fragment (21-229) having a molecular weight of 23.3kDa. The EBI3 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
EBI3 Human Recombinant was lyophilized from a solution containing 10mM Acetic Acid and 0.5% Mannitol.
Purity
Greater than 90% as determined by
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Assay data for Human recombinant EBI3 is based upon qualitative binding to anti-EBI3 antibody.More Info
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Introduction
EBI3 has an induced expression in B lymphocytes in reaction to Epstein-Barr virus infection. EBI3 encodes a secreted glycoprotein belonging to the hematopoietin receptor family, and heterodimerizes with a 28 kDa protein to form iIL-27. EBI3 drives rapid clonal expansion of naive cd4(+) t-cells. EBI3 strongly synergizes with IL-12 to activate IFN-gamma production of naive cd4(+) t-cells. EBI3 mediates its biologic effects through the cytokine receptor wsx-1/tccr.
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Synonyms
Interleukin-27 subunit beta, IL-27 subunit beta, IL-27B, Epstein-Barr virus-induced gene 3 protein, EBV-induced gene 3 protein, EBI3, IL27B.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized EBI3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EBI3 should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized EBI3 in sterile 10mM Acetic acid not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
RKGPPAALTLPRVQCRASRYPIAVDCSWTLPPAPNSTSPVSF
IATYRLGMAARGHSWPCLQQTPTSTSCTITDVQLFSMAPYVL
NVTAVHPWGSSSSFVPFITEHIIKPDPPEGVRLSPLAERQLQ
VQWEPPGSWPFPEIFSLKYWIRYKRQGAARFHRVGPIEATSF
ILRAVRPRARYYVQVAAQDLTDYGELSDWSLPATATMSLGK. -
Background
Title: Epstein-Barr Virus Induced 3 Human Recombinant: Unveiling its Role in Epstein-Barr Virus-Associated Diseases
Abstract:
Epstein-Barr Virus Induced 3 (EBI3) is a crucial cytokine involved in the immune response against Epstein-Barr virus (EBV) and various other pathogens. This research paper provides an extensive analysis of human recombinant EBI3, focusing on its production, characterization, and potential applications in understanding EBV-associated diseases. The paper highlights the significance of EBI3 in modulating immune responses and explores its role in the pathogenesis of EBV-related malignancies. Furthermore, it discusses ongoing research and clinical trials investigating the therapeutic potential of recombinant EBI3 in immune disorders and cancer. The information presented in this paper aims to enhance our understanding of human recombinant EBI3 and its utility as a research tool and a potential immunotherapeutic agent.Introduction:
Epstein-Barr Virus Induced 3 (EBI3) is a cytokine that plays a critical role in the immune response against EBV. Human recombinant EBI3, produced through genetic engineering techniques, provides a valuable tool for studying its immunomodulatory properties and exploring its potential therapeutic applications.Production and Characterization:
Recombinant EBI3 is typically generated using expression systems such as mammalian cells or bacteria. The protein is then purified and characterized to ensure its structural integrity and functional activity. Rigorous quality control measures are implemented to confirm the specificity and potency of the recombinant EBI3.Role in EBV-Associated Diseases:
EBI3 is involved in the regulation of immune responses during EBV infection. It acts as a subunit of the heterodimeric cytokine interleukin-27 (IL-27), which plays a crucial role in anti-viral immunity. Recombinant EBI3 serves as a valuable tool for investigating the mechanisms underlying EBI3-mediated immune regulation and its potential implications in EBV-associated diseases, including infectious mononucleosis, nasopharyngeal carcinoma, and EBV-related lymphomas.Therapeutic Implications:
Dysregulation of the immune response is implicated in various immune disorders and cancers. Recombinant EBI3 holds promise as a potential immunotherapeutic agent due to its immunomodulatory properties. Ongoing research and clinical trials are investigating the therapeutic applications of recombinant EBI3 in conditions such as autoimmune diseases, viral infections, and cancer.Conclusion:
Human recombinant EBI3 represents a valuable research tool and a potential immunotherapeutic agent. Its production, characterization, and applications in understanding EBV-associated diseases contribute to our understanding of immune regulation and the development of targeted therapeutic interventions. Continued research and clinical trials exploring the therapeutic potential of recombinant EBI3 offer promising avenues for improving outcomes in immune disorders and EBV-related malignancies.What is the molecular weight/Mw of EBI3 Protein?
EBI3 Protein has a total Mw of 23.3kDa.
What is the source or expression system of EBI3 Protein?
Escherichia Coli.
What is the Purity of EBI3 Protein?
EBI3 Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of EBI3 Protein?
Assay data for Human recombinant EBI3 is based upon qualitative binding to anti-EBI3 antibody.
What is the amino acid sequence of EBI3 Protein?
RKGPPAALTLPRVQCRASRYPIAVDCSWTLPPAPNSTSPVSF
IATYRLGMAARGHSWPCLQQTPTSTSCTITDVQLFSMAPYVL
NVTAVHPWGSSSSFVPFITEHIIKPDPPEGVRLSPLAERQLQ
VQWEPPGSWPFPEIFSLKYWIRYKRQGAARFHRVGPIEATSF
ILRAVRPRARYYVQVAAQDLTDYGELSDWSLPATATMSLGK.
What applications can EBI3 Protein be used in?
EBI3 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for EBI3 Protein?
The endotoxin level is minimal, EBI3 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.
- View Data Sheet
Name :
VEGF Mouse (121 a.a.), YeastDescription:
Vascular Endothelial Growth Factor (121 a.a.) Mouse Recombinant, Yeast
Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.
Product # :
CYT-1125Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Vascular Endothelial Growth Factor (121 a.a.) Mouse Recombinant produced in yeast is a disulfide-linked homodimer consisting of 2x121 amino acid polypeptide chains, having a molecular mass of approximately 20.7kDa each.VEGF (121 a.a.) is purified by proprietary chromatographic techniques.
Source
Saccharomyces cerevisiae
Formulation
Lyophilized from a 0.2μm filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The activity was measured in a cell proliferation assay using HUVEC human umbilical vein endothelial cells and was found to be 1-4 ng/ml.
More Info
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Introduction
Vascular endothelial growth factor is an important signaling protein involved in both angiogenesis and vasculogenesis.VEGF activity has been mostly studied on cells of the vascular endothelium, although it does have effects on a number of other cell types (e.g. stimulation monocyte/macrophage migration, neurons, cancer cells, kidney epithelial cells ).VEGF mediates increased vascular permeability, induces angiogenesis, vasculogenesis and endothelial cell growth, promotes cell migration, and inhibits apoptosis. In vitro, VEGF has been shown to stimulate endothelial cell mitogenesis and cell migration. VEGF is also a vasodilator and increases microvascular permeability and was originally referred to as vascular permeability factor.
Elevated levels of VEGF is linked to POEMS syndrome, also known as Crow-Fukase syndrome. Mutations in VEGF have been associated with proliferative and nonproliferative diabetic retinopathy. -
Synonyms
Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized VEGF (121 a.a.) although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Vascular Endothelial Growth Factor (121 a.a.) should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Vascular Endothelial Growth Factor (121 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
MAPTTEGEQK SHEVIKFMDV YQRSYCRPIE TLVDIFQEYP DEIEYIFKPS CVPLMRCAGC CNDEALECVP TSESNITMQI MRIKPHQSQH IGEMSFLQHS RCECRPKKDR TKPEKCDKPR R.
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 :
EPYC HumanDescription:
Epiphycan Human Recombinant
Epiphycan, SLRR3B, DSPG3, EPYC Dermatan sulfate proteoglycan 3, Proteoglycan-Lb, PG-Lb, Small chondroitin/dermatan sulfate proteoglycan, PGLB, epiphycan proteoglycan.
Product # :
PRO-2778Price :
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Description
EPYC Human Recombinant produced in HEK293 Cells.is a single, glycosylated polypeptide chain containing 309 amino acids (20-322 a.a.) and having a molecular mass of 35.5kDa. EPYC is fused to a 6 amino acid His-tag at C-terminus and is purified by proprietary chromatographic techniques.
Source
HEK293 Cells.
Formulation
EPYC protein solution (0.5mg/ml) containing 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
>60% and is measured by the ability of the immobilized protein to support the adhesion of Saos‑2 human osteosarcoma cells. When cells are added to human DSPG3 1.25 ug/ml and human fibronectin 0.5 ug/ml coated plates.
More Info
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Synonyms
Epiphycan, SLRR3B, DSPG3, EPYC Dermatan sulfate proteoglycan 3, Proteoglycan-Lb, PG-Lb, Small chondroitin/dermatan sulfate proteoglycan, PGLB, epiphycan proteoglycan.
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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
APTLESINYD SETYDATLED LDNLYNYENI PVDKVEIEIA TVMPSGNREL LTPPPQPEKA QEEEEEEEST PRLIDGSSPQ EPEFTGVLGP HTNEDFPTCL LCTCISTTVY CDDHELDAIP PLPKNTAYFY SRFNRIKKIN KNDFASLSDL KRIDLTSNLI SEIDEDAFRK LPQLRELVLR DNKIRQLPEL PTTLTFIDIS NNRLGRKGIK QEAFKDMYDL HHLYLTDNNL DHIPLPLPEN LRALHLQNNN ILEMHEDTFC NVKNLTYIRK ALEDIRLDGN PINLSKTPQA YMCLPRLPVG SLVHHHHHH.
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Background
Epiphycan, a small leucine-rich proteoglycan, has gained recognition as a crucial player in tissue development, repair, and homeostasis. This research aims to explore the significance of epiphycan and its potential therapeutic applications in various physiological and pathological contexts. By investigating the properties and functions of epiphycan, we can uncover new insights into its role in tissue biology and its potential as a target for therapeutic interventions.
Epiphycan is a proteoglycan primarily expressed in skeletal tissues, such as the growth plate of long bones, articular cartilage, and intervertebral discs. It is an extracellular matrix component that interacts with various growth factors, cytokines, and other matrix proteins, influencing cell behavior and tissue organization. The unique structure of epiphycan, comprising a core protein and attached glycosaminoglycan chains, endows it with diverse regulatory functions.
The involvement of epiphycan in tissue development and repair has been highlighted in several studies. It plays a critical role in chondrogenesis, modulating the differentiation and proliferation of chondrocytes. Furthermore, epiphycan has been implicated in the maintenance of articular cartilage integrity and the prevention of osteoarthritis progression. Its ability to interact with growth factors, such as transforming growth factor-beta (TGF-β) and bone morphogenetic proteins (BMPs), suggests its potential as a modulator of tissue regeneration and repair.
This research will delve into the molecular mechanisms underlying epiphycan's functions and its interactions with various signaling pathways. The paper will explore the regulatory effects of epiphycan on cell behavior, matrix remodeling, and tissue architecture. Additionally, it will examine the implications of epiphycan dysregulation in pathological conditions, such as osteoarthritis, and discuss its potential as a therapeutic target for promoting tissue regeneration and repair.
The study will also investigate the diagnostic and prognostic value of epiphycan in various diseases and conditions. Understanding the expression patterns and alterations of epiphycan in different tissues and disease states may provide valuable insights into disease progression and aid in the development of personalized treatment strategies.
By unraveling the multifaceted roles of epiphycan in tissue biology and its potential therapeutic applications, this research aims to contribute to our understanding of tissue development and repair mechanisms. Furthermore, it highlights the potential of epiphycan as a target for therapeutic interventions and emphasizes the importance of further investigations to harness its full therapeutic potential.
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 :
IMPAD1 Mouse BioactiveDescription:
Inositol Monophosphatase Domain Containing 1 Mouse Recombinant Bioactive
Inositol monophosphatase 3, IMP 3, IMPase 3, Golgi 3-prime phosphoadenosine 5-prime phosphate 3-prime phosphatase, Golgi-resident PAP phosphatase, gPAPP, Inositol monophosphatase domain-containing protein 1, Inositol-1(or 4)-monophosphatase 3, Myo-inositol monophosphatase A3.
Product # :
PRO-2380Price :
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Description
IMPAD1 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 332 amino acids (34-356a.a.) and having a molecular mass of 36.2kDa. (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). IMPAD1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
IMPAD1 protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 5,000 pmol/min/ug and is defined as the amount of enzyme that hydrolyze Adenosine 3, 5-diphosphate per minute at pH 7.5 at 25C.More Info
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Introduction
Inositol monophosphatase 3 (IMPAD1) belongs to the inositol monophosphatase family. IMPAD1 is restricted to the Golgi apparatus and catalyzes the hydrolysis of phosphoadenosine phosphate (PAP) to adenosine monophosphate (AMP). IMPAD1 gene mutations cause the GRAPP type chondrodysplasia with joint dislocations, and a pseudogene of the IMPAD1 gene is located on the long arm of chromosome 1.
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Synonyms
Inositol monophosphatase 3, IMP 3, IMPase 3, Golgi 3-prime phosphoadenosine 5-prime phosphate 3-prime phosphatase, Golgi-resident PAP phosphatase, gPAPP, Inositol monophosphatase domain-containing protein 1, Inositol-1(or 4)-monophosphatase 3, Myo-inositol monophosphatase A3.
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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
ADPGRFSLFG LGSEPAAGEA EVASDGGTVD LREMLAVAVL AAERGGDEVR RVRESNVLHE KSKGKTREGA DDKMTSGDVL SNRKMFYLLK TAFPNVQINT EEHVDASDKE VIVWNRKIPE DILKEIAAPK EVPAESVTVW IDPLDATQEY TEDLRKYVTT MVCVAVNGKP VLGVIHKPFS EYTAWAMVDG GSNVKARSSY NEKTPKIIVS RSHAGMVKQV ALQTFGNQTS IIPAGGAGYK VLALLDVPDM TQEKADLYIH VTYIKKWDIC AGNAILKALG GHMTTLNGEE ISYTGSDGIE GGLLASIRMN HQALVRKLPD LEKSGHHHHH 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 :
TROVE2 HumanDescription:
TROVE Domain Family Member 2 Human Recombinant
60 kDa SS-A/Ro ribonucleoprotein, 60 kDa ribonucleoprotein Ro, RoRNP, 60 kDa Ro protein, Ro 60 kDa autoantigen, TROVE domain family member 2, Sjoegren syndrome type A antigen, SS-A, Sjoegren syndrome antigen A2, TROVE2, RO60, SSA2, RO-60.
Product # :
PRO-329Price :
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Description
RO-60 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain having a molecular mass of 60kDa. RO60 is fused to a 6 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein solution contains 6M Urea, 500mM NaCl, 500mM imidazole and 10mM Tris pH-6.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Ro 60 kDa autoantigen is an RNA-binding protein that binds to several small cytoplasmic RNA molecules known as Y RNAs. SSA2 may stabilize these RNAs from degradation. Sera taken from patients with Systemic Lupus Erythematosus (SLE) often contains antibodies that react with the normal cellular SSA2 protein as if this antigen was foreign.
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Synonyms
60 kDa SS-A/Ro ribonucleoprotein, 60 kDa ribonucleoprotein Ro, RoRNP, 60 kDa Ro protein, Ro 60 kDa autoantigen, TROVE domain family member 2, Sjoegren syndrome type A antigen, SS-A, Sjoegren syndrome antigen A2, TROVE2, RO60, SSA2, RO-60.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
RO-60 although stable at 4°C for 3 weeks, should be stored below -18°C. Please prevent freeze-thaw cycles.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
LYVE1 Human 25-235 a.a.Description:
Lymphatic Vessel Endothelial Hyaluronic Acid Receptor 1 (25-235 a.a) Human Recombinant
HAR, XLKD1, LYVE-1, CRSBP-1, LYVE1, Lymphatic vessel endothelial hyaluronic acid receptor 1 precursor, Cell surface retention sequence-binding protein 1, Hyaluronic acid receptor, Extracellular link domain-containing protein.
Product # :
PKA-349Price :
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Description
LYVE1 Human Recombinant produced in insect cells is a single, glycosylated polypeptide chain containing 229 amino acids and having a molecular mass of 24.8 kDa. As a result of glycosylation, the LYVE1 migrates on SDS-PAGE at approximately 50 kDa. LYVE1 is expressed with 15 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
High Five insect cells.
Formulation
The LYVE1 protein solution contains 20mM Tris buffer pH-7.5 and 10% Glycerol.
Purity
Greater than 90.0% as determined by:(a) Analysis by RP-HPLC.(b) Analysis by SDS-PAGE.
More Info
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Introduction
LYVE1 is a selective marker of the lymphatic endothelium & a surface endocytic receptor for both soluble and immobilized hyaluronan, LYVE1 is an extracellular glycosaminoglycan that plays a role in cell adhesion and migration. LYVE1 functions in lympathic hyaluronan transport and is involved in tumor metastasis. Recombinant human LYVE1 was expressed in and purified by conventional chromatography techniques. The normal adult human choroid is endowed with a significant number of LYVE-1 positive macrophages. LYVE-1 is expressed in a reticulum cell neoplasm in an axillary lymph node. This reticulum cell sarcoma is a lymphatic sinus lining cell sarcoma which might represent another subtype of reticulum cell sarcomas.
LYVE-1 immunohistochemistry is a functional method for detecting lymphatics invaded by cancer cells, and detailed examination of the submucosa around the tumor is important for predicting LN metastasis. -
Synonyms
HAR, XLKD1, LYVE-1, CRSBP-1, LYVE1, Lymphatic vessel endothelial hyaluronic acid receptor 1 precursor, Cell surface retention sequence-binding protein 1, Hyaluronic acid receptor, Extracellular link domain-containing protein.
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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
DPLRAEELS IQVSCRIMGI TLVSKKANQQ LNFTEAKEAC RLLGLSLAGK DQVETALKAS FETCSYGWVG DGFVVISRIS PNPKCGKNGV GVLIRKVPVS RQFAAYCYNS SDTWTNSCIP EIITTKDPIF NTQTATQTTE FIVSDSTYSV ASPYSTIPAP TTTPPAPAST SIPRRKKLIC VTEVFMETST MSTETEPFVE NKAAFKNEAA GFGGSGRLVP RGSHHHHHH.
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 :
KLK3 Human, HEKDescription:
Kallikrein-3 Human Recombinant, HEK
Prostate-specific antigen, PSA, Gamma-seminoprotein, Seminin, Kallikrein-3, P-30 antigen, Semenogelase, KLK3, APS, hK3, KLK2A1
Product # :
ENZ-1149Price :
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Description
KLK3 Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (18-261 a.a) containing a total of 250 amino acids, having a molecular mass of 27.6kDa.KLK3 is fused to a 6 amino acid His-tag at C-terminus,and is purified by proprietary chromatographic techniques.
Source
HEK293 Cells.
Formulation
The KLK3 solution (0.25mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 250pmol/min/ug. Defined by the amount of enzyme that cleaves 1pmole of Succinyl-ArgPro-Tyr-p-Nitroanilide to Succinyl-Arg-Pro-Tyr and p-Nitroanilide per minute at pH 7.5 at 37˚C.
More Info
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Introduction
Kallikrein-3 or KLK3 is a serine proteases subgroup, enzymes can cleave peptide bonds. KLK3 is found in the prostate and may be hold accountable to the regulation of semen liquefaction via seminogelin hydrolysis. The protein is expressed in low concentrations in men with healthy prostates serum. When elevated quantities are found it may show prostate cancer or different prostate disorders such as prostatitis and benign prostatic hyperplasia.
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Synonyms
Prostate-specific antigen, PSA, Gamma-seminoprotein, Seminin, Kallikrein-3, P-30 antigen, Semenogelase, KLK3, APS, hK3, KLK2A1
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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
APLILSRIVG GWECEKHSQP WQVLVASRGR AVCGGVLVHP QWVLTAAHCI RNKSVILLGR HSLFHPEDTG QVFQVSHSFP HPLYDMSLLK NRFLRPGDDS SHDLMLLRLS EPAELTDAVK VMDLPTQEPA LGTTCYASGW GSIEPEEFLT PKKLQCVDLH VISNDVCAQV HPQKVTKFML CAGRWTGGKS TCSGDSGGPL VCNGVLQGIT SWGSEPCALP ERPSLYTKVV HYRKWIKDTI VANPHHHHHH
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 :
EFNB1 HumanDescription:
Ephrin-B1 Human Recombinant
ephrin-B1, LERK2, EPLG2, Elk-L, EPH-related receptor tyrosine kinase ligand 2, EFL-3, ELK ligand, CFND, CFNS, Craniofrontonasal Syndrome (craniofrontonasal dysplasia), MGC8782.
Product # :
PRO-918Price :
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Description
EFNB1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 231 amino acids (28-237) and having a molecular mass of 25.3 kDa.The EFNB1 is fused to a 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The EFNB1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 5% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
EFNB1 is a member of the Eph family. The cell-surface proteins Ephrins split into two groups, ephrin-A and ephrin-B, based on their structure and function and perform as ligands for Eph receptors. The transmembrane EFNB1 proteins have conserved cytoplasmic tyrosine residues that are phosphorylated upon interaction with an EphB receptor. In addition, EFNB1 transduces outside-in signals by C-terminal protein interfaces which influence integrin-mediated cell attachment and migration.
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Synonyms
ephrin-B1, LERK2, EPLG2, Elk-L, EPH-related receptor tyrosine kinase ligand 2, EFL-3, ELK ligand, CFND, CFNS, Craniofrontonasal Syndrome (craniofrontonasal dysplasia), MGC8782.
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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 MLAKNLEPVS WSSLNPKFLS GKGLVIYPKI GDKLDIICPR AEAGRPYEYY KLYLVRPEQA AACSTVLDPN VLVTCNRPEQ EIRFTIKFQE FSPNYMGLEF KKHHDYYITS TSNGSLEGLE NREGGVCRTR TMKIIMKVGQ DPNAVTPEQL TTSRPSKEAD NTVKMATQAP GSRGSLGDSD GKHETVNQEE KSGPGASGGS SGDPDGFFNS K
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.