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1000 results found for “Dysbindin”
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Name :
PVALB HumanDescription:
Parvalbumin Human Recombinant
Parvalbumin alpha, PVALB, D22S749, MGC116759.
Product # :
PRO-004Price :
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Shipped with Ice Packs
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Description
PVALB Human Recombinant fused with a 24 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 134 amino acids (1-110 a.a.) and having a molecular mass of 14.6kDa. The PVALB is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PVALB solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 50mM NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Parvalbumin alpha (PVALB) is a member of a larger group of EF hand proteins. PVALB is a high affinity calcium ion-binding protein which is structurally and functionally similar to calmodulin and troponin C. Parvalbumin is expressed in a specific population of GABAergic interneurones which are believed to have a role in maintaining the balance between excitation and inhibition in the cortex as well as the hippocampus.
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Synonyms
Parvalbumin alpha, PVALB, D22S749, MGC116759.
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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 MGSHMSMTDL LNAEDIKKAV GAFSATDSFD HKKFFQMVGLKKKSADDVKK VFHMLDKDKS GFIEEDELGF ILKGFSPDAR DLSAKETKML MAAGDKDGDG KIGVDEFSTL VAES.
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 :
MBP (27-396) E.ColiDescription:
Maltose Binding Protein (27-396) E.coli Recombinant
Maltose-binding periplasmic protein, MBP, MMBP, Maltodextrin-binding protein, malE, b4034, JW3994.
Product # :
PRO-2321Price :
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Description
Recombinant E.Coli MBP produced in E.Coli is a single, non-glycosylated polypeptide chain containing 371 amino acids (27-396 a.a) and having a molecular mass of 40.8kDa. MBP protein was purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MBP protein solution (1mg/ml) containing phosphate buffered saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Maltose Binding Protein is a member of the maltose/maltodextrin system of E.Coli, which is accountable for the uptake and efficient catabolism of maltodextrins. The maltose/maltodextrin is a complex regulatory and transport system involving many proteins and protein complexes.
MBP elevates the yield of its fusion partner in many cases and is often able to promote the solubility of polypeptides to which it is fused. -
Synonyms
Maltose-binding periplasmic protein, MBP, MMBP, Maltodextrin-binding protein, malE, b4034, JW3994.
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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
MKIEEGKLVI WINGDKGYNG LAEVGKKFEK DTGIKVTVEH PDKLEEKFPQ VAATGDGPDI IFWAHDRFGG YAQSGLLAEI TPDKAFQDKL YPFTWDAVRY NGKLIAYPIA VEALSLIYNK DLLPNPPKTW EEIPALDKEL KAKGKSALMF NLQEPYFTWP LIAADGGYAF KYENGKYDIK DVGVDNAGAK AGLTFLVDLI KNKHMNADTD YSIAEAAFNK GETAMTINGP WAWSNIDTSK VNYGVTVLPT FKGQPSKPFV GVLSAGINAA SPNKELAKEF LENYLLTDEG LEAVNKDKPL GAVALKSYEE ELAKDPRIAA TMENAQKGEI MPNIPQMSAF WYAVRTAVIN AASGRQTVDE ALKDAQTRIT 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.
- View Data Sheet
Name :
RBM3 HumanDescription:
RNA Binding Motif Protein 3 Human Recombinant
IS1-RNPL, RNPL, RNA-binding motif protein 3, Putative RNA-Binding Protein 3, RNA Binding Motif (RNP1, RRM) Protein 3.
Product # :
PRO-1462Price :
Quantity :
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Shipped with Ice Packs
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Description
RBM3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 180 amino acids (1-157 a.a) and having a molecular mass of 19kDa. RBM3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
RBM3 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol and 5mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
RBM3 belongs to the glycine-rich RNA-binding protein family and encodes a protein with one RNArecognition motif (RRM) domain. By cold shock and low oxygen tension the expression of this gene is induced. On chromosome 1 a pseudogene exists. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.Diseases associated with RBM3 include vaccinia, andcryptorchidism. GO annotations linked to this gene include RNA binding and ribosomal large subunit binding. An important paralog of this gene is RBMY1J.
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Synonyms
IS1-RNPL, RNPL, RNA-binding motif protein 3, Putative RNA-Binding Protein 3, RNA Binding Motif (RNP1, RRM) Protein 3.
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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 MGSMSSEEGK LFVGGLNFNT DEQALEDHFS SFGPISEVVV VKDRETQRSR GFGFITFTNP EHASVAMRAM NGESLDGRQI RVDHAGKSAR GTRGGGFGAH GRGRSYSRGG GDQGYGSGRY YDSRPGGYGY GYGRSRDYNG RNQGGYDRYS GGNYRDNYDN
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 :
RNF181 HumanDescription:
Ring Finger Protein 181 Human Recombinant
Ring Finger Protein 181, E3 Ubiquitin-Protein Ligase RNF181, HSPC238, EC 6.3.2.-.
Product # :
PRO-1218Price :
Quantity :
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Shipped with Ice Packs
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Description
RNF181 Human Recombinant produced in E. coli is a single polypeptide chain containing 176 amino acids (1-153) and having a molecular mass of 20.3 kDa.RNF181 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The RNF181 solution (1mg/1ml) 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
E3 ubiquitin-protein ligase RNF181 (RNF181) accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the thioester form and subsequently directly transfers the ubiquitin to targeted substrates. RNF181 is widely expressed, with the highest levels in the liver and heart and the lowest levels in the brain and skeletal muscle. RNF181 is also expressed in platelets (at protein level).
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Synonyms
Ring Finger Protein 181, E3 Ubiquitin-Protein Ligase RNF181, HSPC238, EC 6.3.2.-.
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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 MGSMASYFDE HDCEPSDPEQ ETRTNMLLEL ARSLFNRMDF EDLGLVVDWD HHLPPPAAKT VVENLPRTVI RGSQAELKCP VCLLEFEEEE TAIEMPCHHL FHSSCILPWL SKTNSCPLCR YELPTDDDTY EEHRRDKARK QQQQHRLENL HGAMYT.
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 :
ACTN1 HumanDescription:
Actinin Alpha 1 Human Recombinant
ACTN1, Actinin, Alpha 1, Alpha-Actinin Cytoskeletal Isoform, F-Actin Cross-Linking Protein, Non-Muscle Alpha-Actinin-1, BDPLT15, Actinin 1 Smooth Muscle, Alpha-Actinin-1.
Product # :
PRO-2227Price :
Quantity :
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Shipped with Ice Packs
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Description
ACTN1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 274 amino acids (1-249 a.a) and having a molecular mass of 31.4kDa. ACTN1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ACTN1 protein solution (1mg/ml) containing Phosphate Buffered Saline (pH7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
ACTN1 encodes a nonmuscle, cytoskeletal, alpha actinin isoform and maps to the same site as the structurally similar erythroid beta spectrin gene. Alpha actinins belong to the spectrin gene superfamily which represents a diverse group of cytoskeletal proteins, including the alpha and beta spectrins and dystrophins. Alpha actinin is an actin-binding protein with multiple roles in different cell types. In nonmuscle cells, the cytoskeletal isoform is found along microfilament bundles and adherens-type junctions, where it is involved in binding actin to the membrane. In contrast, skeletal, cardiac, and smooth muscle isoforms are localized to the Z-disc and analogous dense bodies, where they help anchor the myofibrillar actin filaments.
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Synonyms
ACTN1, Actinin, Alpha 1, Alpha-Actinin Cytoskeletal Isoform, F-Actin Cross-Linking Protein, Non-Muscle Alpha-Actinin-1, BDPLT15, Actinin 1 Smooth Muscle, Alpha-Actinin-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 MGSEFMDHYD SQQTNDYMQP EEDWDRDLLL DPAWEKQQRK TFTAWCNSHL RKAGTQIENI EEDFRDGLKL MLLLEVISGE RLAKPERGKM RVHKISNVNK ALDFIASKGV KLVSIGAEEI VDGNVKMTLG MIWTIILRFA IQDISVEETS AKEGLLLWCQ RKTAPYKNVN IQNFHISWKD GLGFCALIHR HRPELIDYGK LRKDDPLTNL NTAFDVAEKY LDIPKMLDAE DIVGTARPDE KAIMTYVSSF YHAF.
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 :
PRLR Human, AntagonistDescription:
Prolactin Receptor Antagonist Human Recombinant
Mammotropin, Luteotropic hormone, Luteotropin, PRL.
Product # :
CYT-1254Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Prolactin Human Receptor Antagonist del 1-9, G129R mutant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 190 amino acids + an additional Ala at n-terminal and having a molecular mass of ~ 22 kDa. The Human Prolactin Receptor Antagonist is purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The protein was lyophilized from a concentrated (1-2mg/ml) solution with 0.02% -0.03% NaHCO3.
Purity
Greater than 97.0% as determined by:
(a) Analysis by Gel Filtration.
(b) Analysis by SDS-PAGE.
Biological Activity
fully biologically active as evidenced by inhibiting PRLR-induced proliferation of Nb2 cells or Baf3 cells stably transfected with hPRL receptors. It also interacts at 1:1 molar ratio with human prolactin receptor extracellular domain as documented by SEC and SPR (Biacore analysis).
More Info
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Synonyms
Mammotropin, Luteotropic hormone, Luteotropin, PRL.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized PRLR although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 mg/ml and up to 3 mg/ml and filter sterilization PRLR can be stored at 4C for several weeks. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized PRLR in sterile 0.4% NaHCO3 adjusted to pH 8-9 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 six N-terminal amino acids was determined and was found to be Ala-Arg-Ser-Gln-Val-Thr
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Background
Prolactin is a pituitary hormone which takes part in the stimulation of milk production, salt and water regulation, development, growth and reproduction. The primary step in its action is binding a specific membrane receptor (prolactin receptor) which belongs to the superfamily of class 1 cytokine receptors. PRLR varies in size (short and long forms) with tissue source and species, from ~40 kDa to 100 kDa. The PRL-R consists of at least 3 separate domains: an extracellular region with 5 cysteines which contains the prolactin binding site, a single transmembrane domain and a cytoplasmic region, the length of which appears to influence ligand binding and regulate cellular function.
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 :
RERG HumanDescription:
RAS-like, Estrogen-Regulated, Growth Inhibitor Human Recombinant
Ras-related and estrogen-regulated growth inhibitor, RERG, MGC15754.
Product # :
PRO-106Price :
Quantity :
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Shipped with Ice Packs
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Description
RERG Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 219 amino acids (1-199 a.a.) and having a molecular mass of 24.7kDa (Molecular size on SDS-PAGE will appear higher). The RERG is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The RERG solution (0.25 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 5mM DTT and 50% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
RERG is a 199 amino acid protein which localizes in the cytoplasm and is a member of the Ras subfamily of small GTPases. RERG is expressed in the pancreas, liver, skin, lung, brain, kidney and heart tissue. RERG is a vital mediator of diverse cell signaling pathways, including those leading to cell proliferation, cytoskeletal organization and secretion.
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Synonyms
Ras-related and estrogen-regulated growth inhibitor, RERG, MGC15754.
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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 MAKSAEVKLA IFGRAGVGKS ALVVRFLTKR FIWEYDPTLE STYRHQATID DEVVSMEILD TAGQEDTIQR EGHMRWGEGF VLVYDITDRG SFEEVLPLKN ILDEIKKPKN VTLILVGNKA DLDHSRQVST EEGEKLATEL ACAFYECSAC TGEGNITEIF YELCREVRRR RMVQGKTRRR SSTTHVKQAI NKMLTKISS.
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 :
Bet v 2.0101Description:
Profilin-1 Recombinant
Profilin-1, Allergen Bet v II, Pollen allergen Bet v 2, Bet v 2, BETVII, Bet v 2.0101.
Product # :
PRO-2283Price :
Quantity :
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Shipped with Ice Packs
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Description
Recombinant Profilin-1 produced in E.coli is a non-glycosylated, polypeptide chain having a calculated molecular mass of 15,625 Dalton. Bet v 2.0101 is expressed with a 10xHis tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Bet v 2.0101 is supplied in 20mM HEPES buffer pH-7.9 and 6M Urea.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
Profilin-1 (Bet v 2.0101) binds to actin and affects the structure of the cytoskeleton. At high concentrations, profiling-1 averts the polymerization of actin, whereas it augments it at low concentrations. By binding to PIP2, Profilin-1 inhibits the creation of IP3 and DG.
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Synonyms
Profilin-1, Allergen Bet v II, Pollen allergen Bet v 2, Bet v 2, BETVII, Bet v 2.0101.
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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 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 :
SDF 1a RatDescription:
Stromal Cell-Derived Factor-1 alpha Rat Recombinant (CXCL12)
SDF-1, CXCL12, Pre-B cell growth-stimulating factor, PBSF, hIRH, chemokine (C-X-C motif) ligand 12, SDF1, SDF1A, TPAR1, SCYB12, SDF-1a, TLSF-a, 12-O-tetradecanoylphorbol 13-acetate repressed protein 1, Thymic lymphoma cell-stimulating factor, TLSF.
Product # :
CHM-354Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Stromal Cell-Derived Factor-1 alpha Rat Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 68 amino acids and having a molecular mass of 7.9 kDa. The SDF-1a is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CXCL12 protein was lyophilized from a concentrated (1 mg/ml) sterile solution containing 20mM Phosphate buffer pH-7.4 and 150mM NaCl.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The specific activity as determined by its ability to chemoattract human peripheral blood monocytes at 50-100ng/ml corresponding to a Specific Activity of 10,000-20,000IU/mg.More Info
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Introduction
SDF-1 (stromal cell-derived factor-1) is small cytokine belonging to the chemokine family that is officially designated Chemokine (C-X-C motif) ligand 12 (CXCL12). It is produced in two forms, SDF-1?/CXCL12a and SDF-1?/CXCL12b, by alternate splicing of the same gene. Chemokines are characterized by the presence of four conserved cysteines, which form two disulfide bonds. The CXCL12 proteins belong to the group of CXC chemokines, whose initial pair of cysteines are separated by one intervening amino acid. CXCL12 is strongly chemotactic for lymphocytes and has been implicated as an important cell co-ordinator during development. During embryogenesis it directs the migration of hematopoietic cells from foetal liver to bone marrow. Mice which were knocked-out for CXCL12 gene were lethal before the birth or within just 1 hour of life. As another role, CXCL12a alters also the electrophysiology of neurons. CXCL12 was shown to be expressend in many tissues in mice (including brain, thymus, heart, lung, liver, kidney, spleen and bone marrow).
The receptor for this chemokine is CXCR4, which was previously called fusin. This CXCL12-CXCR4 interaction used to be considered exclusive (unlike for other chemokines and their receptors), but recently it was suggested that CXCL12 is also bound by CXCR7 receptor.
The gene for CXCL12 is located on human chromosome 10. In human and mouse both CXCL12 and CXCR4 show high identity of sequence: 99% and 90%, respectively. -
Synonyms
SDF-1, CXCL12, Pre-B cell growth-stimulating factor, PBSF, hIRH, chemokine (C-X-C motif) ligand 12, SDF1, SDF1A, TPAR1, SCYB12, SDF-1a, TLSF-a, 12-O-tetradecanoylphorbol 13-acetate repressed protein 1, Thymic lymphoma cell-stimulating factor, TLSF.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized SDF-1a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL12 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 SDF-1a 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
KPVSLSYRCP CRFFESHVAR ANVKHLKILN TPNCALQIVA RLKSNNRQVC IDPKLKWIQE YLDKALNK.
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 :
MBP (27-392) E.ColiDescription:
Maltose Binding Protein E.coli Recombinant
Product # :
PRO-616Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Maltose Binding Protein E.Coli Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 387 amino acids (27-392) with additional 20aa linker and having a molecular mass of 42kDa.
Source
Escherichia Coli.
Formulation
The Maltose Binding Protein solution (1 mg/ml) contains 20mM Tris-HCl pH-8.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Maltose Binding Protein is a member of the maltose/maltodextrin system of E.Coli, which is accountable for the uptake and efficient catabolism of maltodextrins. The maltose/maltodextrin is a complex regulatory and transport system involving many proteins and protein complexes.
MBP elevates the yield of its fusion partner in many cases and is often able to promote the solubility of polypeptides to which it is fused. -
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
MKIEEGKLVI WINGDKGYNG LAEVGKKFEK DTGIKVTVEH PDKLEEKFPQ VAATGDGPDI IFWAHDRFGG YAQSGLLAEI TPDKAFQDKL YPFTWDAVRY NGKLIAYPIAVEALSLIYNK DLLPNPPKTW EEIPALDKEL KAKGKSALMF NLQEPYFTWP LIAADGGYAF KYENGKYDIK DVGVDNAGAK AGLTFLVDLI KNKHMNADTD YSIAEAAFNK GETAMTINGP WAWSNIDTSK VNYGVTVLPT FKGQPSKPFV GVLSAGINAA SPNKELAKEF LENYLLTDEG LEAVNKDKPL GAVALKSYEE ELAKDPRIAA TMENAQKGEI MPNIPQMSAF WYAVRTAVIN AASGRQTVDE ALKDAQTNSS SNNNNNNNNN NLGIEGR.
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 :
METRN MouseDescription:
Meteorin Mouse Recombinant
Meteorin, Hypoxia/reoxygenation regulatory factor, Metrn, 1810034B16Rik, Hyrac.
Product # :
PRO-2241Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
METRN produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 276 amino acids (22-291 a.a.) and having a molecular mass of 30.2kDa (Migrates at 28-40kDa on SDS-PAGE under reducing conditions). METRN is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
METRN protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Meteorin (METRN) is involved in both glial cell differentiation and axonal network formation during neurogenesis. METRN promotes astrocyte differentiation and transforms cerebellar astrocytes into radial glia. Moreover, the METRN protein stimulates axonal extension in small and intermediate neurons of sensory ganglia by activating nearby satellite glia.
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Synonyms
Meteorin, Hypoxia/reoxygenation regulatory factor, Metrn, 1810034B16Rik, Hyrac.
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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
GYSEDRCSWR GSGLTQEPGS VGQLTLDCTE GAIEWLYPAG ALRLTLGGPD PGTRPSIVCL RPERPFAGAQ VFAERMTGNL ELLLAEGPDL AGGRCMRWGP RERRALFLQA TPHRDISRRV AAFRFELHED QRAEMSPQAQ GLGVDGACRP CSDAELLLAA CTSDFVIHGT IHGVAHDTEL QESVITVVVA RVIRQTLPLF KEGSSEGQGR ASIRTLLRCG VRPGPGSFLF MGWSRFGEAW LGCAPRFQEF SRVYSAALTT HLNPCEMALD 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 :
SERPINA9 MouseDescription:
Serpin Peptidase Inhibitor, Clade A Mouse Recombinant
Serpin A9, Serpina9, SERPINA9.
Product # :
PRO-2366Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SERPINA9 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 401 amino acids (26-418 a.a) and having a molecular mass of 45.2kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).SERPINA9 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
SERPINA9 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
-
Introduction
Serpin Peptidase Inhibitor, Clade A Member 9, also known as serpin A9, belongs to the Serpin superfamily of serine protease inhibitors. Serpins are the most extensively distributed superfamily of protease inhibitors which use a conformational modification to inhibit target enzymes. Serpins are known to inhibit serine proteases as well as inhibiting caspases in addition to papain-like cysteine proteases. Serpins are conformational labile and numerous of the disease-linked mutations of serpins outcome in misfolding or in pathogenic, inactive polymers. serpin A9 demonstrates inhibition towards trypsin, thrombin, as well as plasmin and binds DNA and heparin.
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Synonyms
Serpin A9, Serpina9, SERPINA9.
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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
NPYNQESSHL PSMKKNPASQ VSPSNTRFSF LLYQRLAQEN PGQNILFSPV SISTSLAMLS LGARSATKTQ ILRTLGFNFT WVSEPTIHMG FEYLVRSLNK CHQGRELRMG SVLFIRKELQ LQATFLDRVK KLYGAKVFSE DFSNAATAQA QINSYVEKET KGKVVDVIQD LDSQTAMVLV NHIFFKANWT QPFSTANTNK SFPFLLSKGT TVHVPMMHQT ESFAFGVDKE LGCSILQMDY RGDAVAFFVL PGKGKMRQLE KSLSARRLRK WSRSLQKRWI KVFIPKFSIS ASYNLETILP KMGIRDAFNS NADFSGITKT HFLQVSKAAH KAVLDVSEEG TEAAAATTTK LIVRSRDTPS SIIAFKEPFL ILLLDKNTES VLFLGKVENP RKMLEHHHHH H
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 :
FBLIM1 HumanDescription:
Filamin Binding LIM Protein 1 Human Recombinant
Filamin binding LIM protein 1, CAL, FBLP-1, FBLP1, RP11-169K16.5, Migfilin, Mitogen-inducible 2-interacting protein, MIG2-interacting protein.
Product # :
PRO-1473Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
FBLIM1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 396 amino acids (1-373) and having a molecular mass of 43.1 kDa. FBLIM1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The FBLIM1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Filamin binding LIM protein 1 (FBLIM1) plays a role as an anchoring site for cell-ECM adhesion proteins and filamin-containing actin filaments. FBLIM1 is involved in cell shape spreading and motility. FBLIM1 participates in the regulation of filamin-mediated cross-linking and stabilization of actin filaments. FBLIM1 promotes stimulation of integrins and regulates integrin-mediated cell-cell adhesion.
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Synonyms
Filamin binding LIM protein 1, CAL, FBLP-1, FBLP1, RP11-169K16.5, Migfilin, Mitogen-inducible 2-interacting protein, MIG2-interacting protein.
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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 MGSMASKPEK RVASSVFITL APPRRDVAVA EEVRQAVCEA RRGRPWEAPA PMKTPEAGLA GRPSPWTTPG RAAATVPAAP MQLFNGGCPP PPPVLDGEDV LPDLDLLPPP PPPPPVLLPS EEEAPAPMGA SLIADLEQLH LSPPPPPPQA PAEGPSVQPG PLRPMEEELP PPPAEPVEKG ASTDICAFCH KTVSPRELAV EAMKRQYHAQ CFTCRTCRRQ LAGQSFYQKD GRPLCEPCYQ DTLERCGKCG EVVRDHIIRA LGQAFHPSCF TCVTCARCIG DESFALGSQN EVYCLDDFYR KFAPVCSICE NPIIPRDGKD AFKIECMGRN FHENCYRCED CRILLSVEPT DQGCYPLNNH LFCKPCHVKR SAAGCC.
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 :
CNDP1 Human, ActiveDescription:
CNDP Dipeptidase 1 Human Recombinant, Active
Carnosine Dipeptidase 1 (Metallopeptidase M20 Family), Glutamate Carboxypeptidase-Like Protein 2, CNDP Dipeptidase 1, Serum Carnosinase, Carnosinase 1, CPGL2, CN1, Carnosine Dipeptidase 1, EC 3.4.13.20, HsT2308.
Product # :
ENZ-1022Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CNDP1 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 489 amino acids (27-507 a.a.) and having a molecular mass of 54.9kDa (Migrates at 50-70kDa on SDS-PAGE under reducing conditions).CNDP1 is expressed with a 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Insect cells.
Formulation
CNDP1 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is >3,000 pmol/min/ug, and as measured by the hydrolysis of carnosine per minute at pH6.8 at 25°C.More Info
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Introduction
CNDP Dipeptidase 1, also known as CNDP1 is a member of the peptidase M20A family. CNDP1 Mannheim which is the shortest allelic form has been more common in the absence of nephropathy in addition to being associated with lower serum carnosinase levels. Furthermore, Carnosine inhibited the increased production of fibronectin as well as collagen type VI in podocytes and the increased production of TGF-beta in mesangial cells. Diabetic patients with the CNDP1 Mannheim variant are less at risk for nephropathy. In addition, on renal cells carnosine protects against the adverse effects of high glucose levels.
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Synonyms
Carnosine Dipeptidase 1 (Metallopeptidase M20 Family), Glutamate Carboxypeptidase-Like Protein 2, CNDP Dipeptidase 1, Serum Carnosinase, Carnosinase 1, CPGL2, CN1, Carnosine Dipeptidase 1, EC 3.4.13.20, HsT2308.
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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
SPSPPPALLE KVFQYIDLHQ DEFVQTLKEW VAIESDSVQP VPRFRQELFR MMAVAADTLQ RLGARVASVD MGPQQLPDGQ SLPIPPVILA ELGSDPTKGT VCFYGHLDVQ PADRGDGWLT DPYVLTEVDG KLYGRGATDN KGPVLAWINA VSAFRALEQD LPVNIKFIIE GMEEAGSVAL EELVEKEKDR FFSGVDYIVI SDNLWISQRK PAITYGTRGN SYFMVEVKCR DQDFHSGTFG GILHEPMADL VALLGSLVDS SGHILVPGIY DEVVPLTEEE INTYKAIHLD LEEYRNSSRV EKFLFDTKEE ILMHLWRYPS LSIHGIEGAF DEPGTKTVIP GRVIGKFSIR LVPHMNVSAV EKQVTRHLED VFSKRNSSNK MVVSMTLGLH PWIANIDDTQ YLAAKRAIRT VFGTEPDMIR DGSTIPIAKM FQEIVHKSVV LIPLGAVDDG EHSQNEKINR WNYIEGTKLF AAFFLEMAQL HLEHHHHHH.
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 :
CCL24 MouseDescription:
Eotaxin-2 Mouse Recombinant (CCL24)
C-C motif chemokine 24, Small-inducible cytokine A24, Myeloid progenitor inhibitory factor 2, CK-beta-6, Eosinophil chemotactic protein 2, Eotaxin-2, CCL24, Ckb-6, MPIF2, MPIF-2, SCYA24, Eotaxin2, CCL-24.
Product # :
CHM-368Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
CCL24 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 93 amino acids and having a molecular mass of 10.3 kDa. The CCL24 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CCL24 protein was lyophilized from a concentrated (1mg/ml) sterile solution containing 20mM Phosphate buffer pH-7.4 and 0.15M sodium chloride.
Purity
Greater than 97.0% as determined by:(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Determined by its ability to chemoattract murine lymphocytes using a concentration range of 10-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.More Info
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Introduction
Eotaxin-2, also called MPIF2 & Ckb6, is a novel CC chemokine produced by activated monocytes and T lymphocytes. Eotaxin-2 selectively chemoattracts cells expressing CCR3 including eosinophils, basophils, Th2 T cells, mast cells, and certain subsets of dendritic cells. Furthermore, Eotaxin-2 inhibits the proliferation of multipotential hematopoietic progenitor cells. The mature protein, which includes C-terminal truncation, contains 78 amino acids (92 amino acids for the mouse homolog, without C-terminal truncation).
CCL24 functions as a chemotactic chemokine for resting t-lymphocytes, and eosinophils. CCL24 has lower chemotactic activity for neutrophils but none for monocytes and activated lymphocytes. CCL24 is a strong suppressor of colony formation by a multipotential hematopoietic progenitor cell line and binds to CCR3. -
Synonyms
C-C motif chemokine 24, Small-inducible cytokine A24, Myeloid progenitor inhibitory factor 2, CK-beta-6, Eosinophil chemotactic protein 2, Eotaxin-2, CCL24, Ckb-6, MPIF2, MPIF-2, SCYA24, Eotaxin2, CCL-24.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Eotaxin-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL24 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized CCL24 Mouse Recombinant in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
VTIPSSCCTS FISKKIPENR VVSYQLANGS ICPKAGVIFI TKKGHKICTD PKLLWVQRHI QKLDAKKNQP SKGAKAVRTK FAVQRRRGNS TEV.
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Background
What is the molecular weight/Mw of CCL24 MOUSE Protein?
CCL24 MOUSE Protein has a total Mw of 10.3kDa.
What is the source or expression system of CCL24 MOUSE Protein?
Escherichia Coli.
What is the Purity of CCL24 MOUSE Protein?
CCL24 MOUSE Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of CCL24 MOUSE Protein?
Determined by its ability to chemoattract murine lymphocytes using a concentration range of 10-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.
What is the amino acid sequence of CCL24 MOUSE Protein?
VTIPSSCCTS FISKKIPENR VVSYQLANGS ICPKAGVIFI TKKGHKICTD PKLLWVQRHI QKLDAKKNQP SKGAKAVRTK FAVQRRRGNS TEV.
What applications can CCL24 MOUSE Protein be used in?
CCL24 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CCL24 MOUSE Protein?
The endotoxin level is minimal, CCL24 MOUSE Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Eotaxin MouseDescription:
Eotaxin Mouse Recombinant (CCL11)
Small inducible cytokine A11, CCL11, Eosinophil chemotactic protein, chemokine (C-C motif) ligand 11, SCYA11.
Product # :
CHM-308Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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Description
Eotaxin Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 74 amino acids and having a molecular mass of 8403.2 Dalton. The CCL11 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated (1mg/ml) solution in water containing no additives.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The Biological activity was determined by measuring the dose dependent phosphorylation of ERK1 and ERK2 in CCR3 transfected 293 cells. Significant ERK phosphorylation is observed with >100 ng/ml (corresponding to a Specific Activity of 10,000IU/mg) of recombinant mouse eotaxin.More Info
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Introduction
Chemokine (C-C motif) ligand 11 (CCL11) is a small cytokine belonging to the CC chemokine family that is also known as eotaxin. CCL11 selectively recruits eosinophils by inducing their chemotaxis, and therefore, is implicated in allergic responses. The effects of CCL11 are mediated by its binding to a G-protein-linked receptor known as a chemokine receptor. Chemokine receptors for which CCL11 is a ligand include CCR2, CCR3 and CCR5. The gene for human CCL11 (scya11) is encoded on three exons and is located on chromosome 17.
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Synonyms
Small inducible cytokine A11, CCL11, Eosinophil chemotactic protein, chemokine (C-C motif) ligand 11, SCYA11.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Eotaxin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL11 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 Eotaxin 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 His-Pro-Gly-Ser-Ile.
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Background
What is the molecular weight/Mw of EOTAXIN MOUSE Protein?
EOTAXIN MOUSE Protein has a total Mw of 8.4kDa.
What is the source or expression system of EOTAXIN MOUSE Protein?
Escherichia Coli.
What is the Purity of EOTAXIN MOUSE Protein?
EOTAXIN MOUSE Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of EOTAXIN MOUSE Protein?
The Biological activity was determined by measuring the dose dependent phosphorylation of ERK1 and ERK2 in CCR3 transfected 293 cells. Significant ERK phosphorylation is observed with >100 ng/ml (corresponding to a Specific Activity of 10,000IU/mg) of recombinant mouse eotaxin.
What is the amino acid sequence of EOTAXIN MOUSE Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be His-Pro-Gly-Ser-Ile.
What applications can EOTAXIN MOUSE Protein be used in?
EOTAXIN MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for EOTAXIN MOUSE Protein?
The endotoxin level is minimal, EOTAXIN MOUSE Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Flt3 Ligand Mouse, Sf9Description:
Flt3 Ligand Mouse Recombinant, Sf9
Fms-related tyrosine kinase 3 ligand, Flt3 ligand, Flt3L, SL cytokine, lt3lgF, Flt3l.
Product # :
CYT-910Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Flt3 Ligand produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (27-189 a.a.) and fused to a 6 aa His Tag at C-terminus containing a total of 169 amino acids and having a molecular mass of 19.3kDa.Flt3 Ligand shows multiple bands between 18-28kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
Flt3 Ligand protein solution (0.5mg/ml) contains Phosphate buffered saline (pH7.4) and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
FLT3 ligand is a receptor for the fl cytokine has a tyrosine-protein kinase activity & a growth factor that regulates proliferation of early hematopoietic cells. Flt3-Ligand synergizes with other CSFs and interleukins to induce growth and differentiation.
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Synonyms
Fms-related tyrosine kinase 3 ligand, Flt3 ligand, Flt3L, SL cytokine, lt3lgF, Flt3l.
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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
GTPDCYFSHS PISSNFKVKF RELTDHLLKD YPVTVAVNLQ DEKHCKALWS LFLAQRWIEQ LKTVAGSKMQ TLLEDVNTEI HFVTSCTFQP LPECLRFVQT NISHLLKDTC TQLLALKPCI GKACQNFSRC LEVQCQPDSS TLLPPRSPIA LEATELPEPR PRQHHHHHH
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Background
What is the molecular weight/Mw of FLT3 LIGAND MOUSE, SF9 Protein?
FLT3 LIGAND MOUSE, SF9 Protein has a total Mw of 19.3kDa.
What is the source or expression system of FLT3 LIGAND MOUSE, SF9 Protein?
Sf9, Baculovirus cells.
What is the Purity of FLT3 LIGAND MOUSE, SF9 Protein?
FLT3 LIGAND MOUSE, SF9 Protein is >85% pure as determined by SDS-PAGE.
What is the Biological Activity of FLT3 LIGAND MOUSE, SF9 Protein?
The biological functionality of FLT3 LIGAND MOUSE, SF9 Protein will be determined in the future.
What is the amino acid sequence of FLT3 LIGAND MOUSE, SF9 Protein?
GTPDCYFSHS PISSNFKVKF RELTDHLLKD YPVTVAVNLQ DEKHCKALWS LFLAQRWIEQ LKTVAGSKMQ TLLEDVNTEI HFVTSCTFQP LPECLRFVQT NISHLLKDTC TQLLALKPCI GKACQNFSRC LEVQCQPDSS TLLPPRSPIA LEATELPEPR PRQHHHHHH.
What applications can FLT3 LIGAND MOUSE, SF9 Protein be used in?
FLT3 LIGAND MOUSE, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for FLT3 LIGAND MOUSE, SF9 Protein?
The endotoxin level is minimal, FLT3 LIGAND MOUSE, SF9 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 :
CD105 Human, Sf9Description:
Endoglin Human Recombinant, Sf9
CD105, ENG, END, ORW, HHT1, ORW1, FLJ41744, Endoglin.
Product # :
CYT-389Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
CD105 Human Recombinant extracellular domain produced in baculovirus is a homodimeric, glycosylated, Polypeptide containing 586 amino acids and having a molecular mass of 61 kDa but as a result of glycosylation, migrates at 90 kDa under reducing conditions in SDS-PAGE. The CD105 is fused to a C-terminal His-tag (6xHis) and purified by proprietary chromatographic techniques.
Source
Sf9 Insect Cells.
Formulation
Endoglin was lyophilized from a concentrated (1mg/ml) sterile solution containing 1xPBS.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Measured by its ability to bind with rhTGF-beta RII/Fc in a functional ELISA. Optimal dilutions should be determined by each laboratory for each application.More Info
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Introduction
Endoglin is a type I membrane glycoprotein located on cell surfaces and is part of the TGF beta receptor complex.
The protein consists of a homodimer of 180 kDA with disulfide links. It has been found on endothelial cells, activated macrophages, fibroblasts, and smooth muscle cells. Endoglin has been found to be part of the TGF-beta1 receptor complex. It thus may be involved in the binding of TGF-beta1, TGF-beta3, activin-A, BMP-2, and BMP-7. Beside TGF-beta signaling endoglin may have other functions. It has been postulated that endoglin is involved in the cytoskeletal organization affecting cell morphology and migration. Endoglin has a role in the development of the cardiovascular system and in vascular remodeling. Its expression is regulated during heart development . Experimental mice without the endoglin gene die due to cardiovascular abnormalities. -
Synonyms
CD105, ENG, END, ORW, HHT1, ORW1, FLJ41744, Endoglin.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Endoglin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CD105 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 CD-105 in sterile PBS not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MDRGTLPLAVALLLASCSLSPTSLAETVHCDLQPVGPERGEVTY TTSQVSKGCVAQAPNAILEVHVLFLEFPTGPSQLELTLQASKQNGTWPREVLLVL SVNSSVFLHLQALGIPLHLAYNSSLVTFQEPPGVNTTELPSFPKTQILEWAAERGPI TSAAELNDPQSILLRLGQAQGSLSFCMLEASQDMGRTLEWRPRTPALVRGCHLE GVAGHKEAHILRVLPGHSAGPRTVTVKVELSCAPGDLDAVLILQGPPYVSWLID ANHNMQIWTTGEYSFKIFPEKNIRGFKLPDTPQGLLGEARMLNASIVASFVELPL ASIVSLHASSCGGRLQTSPAPIQTTPPKDTCSPELLMSLIQTKCADDAMTLVLKKE LVAHLKCTITGLTFWDPSCEAEDRGDKFVLRSAYSSCGMQVSASMISNEAVVNI LSSSSPQRKKVHCLNMDSLSFQLGLYLSPHFLQASNTIEPGQQSFVQVRVSPSVSE FLLQLDSCHLDLGPEGGTVELIQGRAAKGNCVSLLSPSPEGDPRFSFLLHFYTVPI PKTGTLSCTVALRPKTGS.
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Background
What is the molecular weight/Mw of CD105 Protein?
CD105 Protein has a total Mw of 90kDa.
What is the source or expression system of CD105 Protein?
Sf9 Insect Cells.
What is the Purity of CD105 Protein?
CD105 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CD105 Protein?
Measured by its ability to bind with rhTGF-beta RII/Fc in a functional ELISA. Optimal dilutions should be determined by each laboratory for each application.
What is the amino acid sequence of CD105 Protein?
MDRGTLPLAVALLLASCSLSPTSLAETVHCDLQPVGPERGEVTY TTSQVSKGCVAQAPNAILEVHVLFLEFPTGPSQLELTLQASKQNGTWPREVLLVL SVNSSVFLHLQALGIPLHLAYNSSLVTFQEPPGVNTTELPSFPKTQILEWAAERGPI TSAAELNDPQSILLRLGQAQGSLSFCMLEASQDMGRTLEWRPRTPALVRGCHLE GVAGHKEAHILRVLPGHSAGPRTVTVKVELSCAPGDLDAVLILQGPPYVSWLID ANHNMQIWTTGEYSFKIFPEKNIRGFKLPDTPQGLLGEARMLNASIVASFVELPL ASIVSLHASSCGGRLQTSPAPIQTTPPKDTCSPELLMSLIQTKCADDAMTLVLKKE LVAHLKCTITGLTFWDPSCEAEDRGDKFVLRSAYSSCGMQVSASMISNEAVVNI LSSSSPQRKKVHCLNMDSLSFQLGLYLSPHFLQASNTIEPGQQSFVQVRVSPSVSE FLLQLDSCHLDLGPEGGTVELIQGRAAKGNCVSLLSPSPEGDPRFSFLLHFYTVPI PKTGTLSCTVALRPKTGS.
What applications can CD105 Protein be used in?
CD105 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CD105 Protein?
The endotoxin level is minimal, CD105 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 :
Adiponectin Mouse, TrimericDescription:
Adiponectin Mouse Recombinant, Trimeric form
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
Product # :
CYT-247Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
Trimeric form of Acrp30 Mouse was expressed in HEK293 cells.The cysteine 39 was replaced with alanine (C39A) 9. mAd-C39A can only form trimer, but not hexamer or HMW form.
Source
HEK293 (Human embryonic kidney cell line).
Formulation
Mouse Acrp30 filtered (0.4µm) and lyophilized from 0.5 mg/ml in 0.05M phosphate buffer, 0.05M NaCl, pH 7.2.
Purity
Acrp30 Mouse purity is greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Adiponectin is a hormone exclusively expressed from adipose tissue. Many studies demonstrate that adiponectin has direct anti-diabetic, anti-atherogenic and anti-inflammatory functions. APM-1 can increase insulin sensitivity of skeletal muscle, attenuate hepatic lipogenesis and luconeogenesis, regulate NO production in endothelial cells, inhibit proliferation of smooth muscle cells and prevent lipid accumulation of macrophage cells.
In the circulation, adiponectin is present as three different oligomeric complexes, including the high molecular weight (HMW), the middle molecular weight (MMW, also called hexamer) and low molecular weigh (MMW, also called trimer) forms 8. Different oligomeric complex of adiponectin activates different signaling pathways and exerts distinct functions. -
Synonyms
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
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Physical Appearance
Filtered white lyophilized (freeze-dried) powder.
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Stability
Store lyophilized Acrp30 Mouse at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted Acrp30 Mouse can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
Add deionized water to prepare a working stock solution of approximately 0.5 mg/mL and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Background
What is the molecular weight/Mw of ADIPONECTIN Protein?
ADIPONECTIN Protein has a total Mw of 26kDa.
What is the source or expression system of ADIPONECTIN Protein?
HEK293
What is the Purity of ADIPONECTIN Protein?
ADIPONECTIN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of ADIPONECTIN Protein?
The biological functionality of ADIPONECTIN Protein will be determined in the future.
What applications can ADIPONECTIN Protein be used in?
ADIPONECTIN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for ADIPONECTIN Protein?
The endotoxin level is minimal, ADIPONECTIN 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 :
Hemopexin Human, Sf9Description:
Hemopexin Human Recombinant, Sf9
Hemopexin, Beta-1B-Glycoprotein, HX, Beta-1B-glycoprotein.
Product # :
PRO-2544Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
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- formulation
- purity
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Description
Hemopexin produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 448 amino acids (24-462a.a.) and having a molecular mass of 50.4kDa. (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).Hemopexin is expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
Hemopexin protein solution (0.5mg/ml) contains 10% glycerol & Phosphate Buffered Saline (pH 7.4).
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Hemopexin (or haemopexin) is a plasma protein that binds heme with the highest affinity of any known protein. Hemopexin is generally expressed in liver, and belongs to acute phase reactants, the synthesis of which is induced after inflammation. Heme is potentially very toxic because of its ability to intercalate into lipid membrane and to generate hydroxyl radicals. Hemopexin’s function of scavenging the heme released or lost by the turnover of heme proteins such as hemoglobin defends the body from the oxidative damage that free heme can cause. Additionally, hemopexin discharges its bound ligand for internalisation upon interacting with a specific receptor located on the surface of liver cells. This hemopexin function is in order to preserve the body's iron. Hemopexin’s levels in the serum are an indication of how much heme is present in the blood. Low Hemopexin levels show that there is a lot of it in the serum. For that reason, low hemopexin levels indicate that there has been consid
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Synonyms
Hemopexin, Beta-1B-Glycoprotein, HX, Beta-1B-glycoprotein.
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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
ADPTPLPPTS AHGNVAEGET KPDPDVTERC SDGWSFDATT LDDNGTMLFF KGEFVWKSHK WDRELISERW KNFPSPVDAA FRQGHNSVFL IKGDKVWVYP PEKKEKGYPK LLQDEFPGIP SPLDAAVECH RGECQAEGVL FFQGDREWFW DLATGTMKER SWPAVGNCSS ALRWLGRYYC FQGNQFLRFD PVRGEVPPRY PRDVRDYFMP CPGRGHGHRN GTGHGNSTHH GPEYMRCSPH LVLSALTSDN HGATYAFSGT HYWRLDTSRD GWHSWPIAHQ WPQGPSAVDA AFSWEEKLYL VQGTQVYVFL TKGGYTLVSG YPKRLEKEVG TPHGIILDSV DAAFICPGSS RLHIMAGRRL WWLDLKSGAQ ATWTELPWPH EKVDGALCME KSLGPNSCSA NGPGLYLIHG PNLYCYSDVE KLNAAKALPQ PQNVTSLLGC THHHHHHH.
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 :
Borrelia Garinii DbpADescription:
Borrelia Garinii Decorin Binding Protein A Recombinant
Product # :
BOR-025Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
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- source
- formulation
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Description
Recombinant Borrelia Garinii Decorin Binding Protein A produced in E.coli is a non-glycosylated, polypeptide chain having a calculated molecular mass of 19kDa. Borrelia Garinii DbpA is expressed with a -10x His tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Borrelia Garinii DbpA 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
Borrelia is a part of the genus of bacteria of the spirochete phylum. Borrelia causes borreliosis, which is a zoonotic, vector-borne disease transmitted mainly by ticks and some by lice, depending on the species. Of the 36 known species of Borrelia, 12 are distinguished to cause Lyme disease or borreliosis and are transmitted by ticks. The main Borrelia species causing Lyme disease are Borrelia burgdorferi, Borrelia afzelii, and Borrelia garinii. Borreliella garinii DbpA demonstrates the typical lipid anchor and decorin/glycoaminoglycon binding properties of a DbpA protein.
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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-type human antibodies.2. Immunodot test with Lyme disease positive/negative plasma.
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Applications
Western blot with Lyme positive plasma.
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 :
SERPINA8 HumanDescription:
Serpin Peptidase Inhibitor, Clade A Member 8 Human Recombinant
Angiotensinogen, Serpin A8, AGT, SERPINA8, ANHU.
Product # :
PRO-1572Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
SERPINA8 Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (a.a 34-485) containing a total of 462 amino acids, having a molecular mass of 51.0kDa (calculated) and fused to a 2 a.a C-terminal linker and an 8 a.a Flag tag at C-Terminus.The Human SERPINA8 is purified by proprietary chromatographic techniques.
Source
HEK 293.
Formulation
Filtered (0.4µm) and lyophilized from 0.5mg/ml in 20mM Tris buffer and 50mM NaCl, pH 7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Serpin Peptidase Inhibitor, Clade A Member 8 (SERPINA8), which is a pre-angiotensinogen or angiotensinogen precursor, is expressed in the liver and cleaved by the enzyme renin in response to lowered blood pressure. The ensuing product, angiotensin I, is at that point cleaved by angiotensin converting enzyme (ACE) to produce the physiologically active enzyme angiotensin II. SERPINA8 protein is involved in maintaining blood pressure and in the pathogenesis of essential hypertension and preeclampsia. SERPINA8 gene mutations are linked with susceptibility to essential hypertension, and may cause renal tubular dysgenesis, which is a severe disorder of renal tubular development. Defects in the SERPINA8 gene are also linked with non-familial structural atrial fibrillation, and inflammatory bowel disease.
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Synonyms
Angiotensinogen, Serpin A8, AGT, SERPINA8, ANHU.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to add deionized water to a working concentration of 0.5mg/ml and let the lyophilized pellet dissolve completely. SERPINA8 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
DRVYIHPFHL VIHNESTCEQ LAKANAGKPK DPTFIPAPIQ AKTSPVDEKA LQDQLVLVAA KLDTEDKLRA AMVGMLANFL GFRIYGMHSE LWGVVHGATV LSPTAVFGTL ASLYLGALDH TADRLQAILG VPWKDKNCTS RLDAHKVLSA LQAVQGLLVA QGRADSQAQL LLSTVVGVFT APGLHLKQPF VQGLALYTPV VLPRSLDFTE LDVAAEKIDR FMQAVTGWKT GCSLTGASVD STLAFNTYVH FQGKMKGFSL LAEPQEFWVD NSTSVSVPML SGMGTFQHWS DIQDNFSVTQ VSFTESACLL LIQPHYASDL DKVEGLTFQQ NSLNWMKKLS PRTIHLTMPQ LVLQGSYDLQ DLLAQAELPA ILHTELNLQK LSNDRIRVGE VLNSIFFELE ADEREPTEST QQLNKPEVLE VTLNRPFLFA VYDQSATALH FLGRVANPLS TART DYKDDD DK.
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 :
DNAJC24 HumanDescription:
DnaJ (Hsp40) Homolog, Subfamily C, Member 24 Human Recombinant
DnaJ homolog subfamily C member 24, DNAJC24, DPH4, JJJ3, ZCSL3, CSL-type zinc finger-containing protein 3, Diphthamide biosynthesis protein 4.
Product # :
HSP-056Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
DNAJC24 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 172 amino acids (1-149 a.a.) and having a molecular mass of 19.5kDa. DNAJC24 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The DNAJC24 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
DnaJ homolog subfamily C member 24 (DNAJC24) belongs to the ZCSL family of proteins and each contain one DPH-type zinc finger. DNAJC24 is involved in the synthesis of diphthamide, a protein found on translation elongation factor EF-2 which is the target of bacterial ADP-ribosylating toxins. DNAJC24 stimulates the ATPase activity of few Hsp70-type chaperones. DNAJC24 detected in heart, brain, spleen, lung, liver, kidney and testis.
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Synonyms
DnaJ homolog subfamily C member 24, DNAJC24, DPH4, JJJ3, ZCSL3, CSL-type zinc finger-containing protein 3, Diphthamide biosynthesis protein 4.
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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 MGSMMAVEQM PKKDWYSILG ADPSANISDL KQKYQKLILM YHPDKQSTDV PAGTVEECVQ KFIEIDQAWK ILGNEETKRE YDLQRCEDDL RNVGPVDAQV YLEEMSWNEG DHSFYLSCRC GGKYSVSKDE AEEVSLISCD TCSLIIELLH YN.
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.