Search: 1000 results found for "erythropoietin"

Description:

Thyroid Hormone Responsive Human Recombinant

Lpgp, LPGP1, S14, SPOT14, THRP, Spot 14 protein.

Product # :

PRO-1485

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Description

THRSP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 169 amino acids (1-146 a.a.) and having a molecular mass of 18.9kDa.THRSP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Thyroid Hormone Responsive (THRSP) is a member of the SPOT14 family. THRSP is similar to the gene product of S14, a rat gene whose expression is limited to liver and adipose tissue and is controlled by nutritional and hormonal factors. THRSP is expressed in liver and adipocytes, specifically in lipomatous modules. In addition It is expressed in lipogenic breast cancers, which suggests a role in controlling tumor lipid metabolism.
Synonyms
Lpgp, LPGP1, S14, SPOT14, THRP, Spot 14 protein.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMQVLTKR YPKNCLLTVM DRYAAEVHNM EQVVMIPSLL RDVQLSGPGG QAQAEAPDLY TYFTMLKAIC VDVDHGLLPR EEWQAKVAGS EENGTAETEE VEDESASGEL DLEAQFHLHF SSLHHILMHL TEKAQEVTRK YQEMTGQVW.

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.

Description:

Ephrin A3 Human Recombinant, Sf9

Ephrin-A3, EFL2, Ehk1-L, EPLG3, LERK3, EPH-related receptor tyrosine kinase ligand 3.

Product # :

PRO-2614

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Description

EFNA3 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 434 amino acids (23-214aa) and having a molecular mass of 48.7kDaEFNA3 is fused to a 242 amino acid hIgG-His-Tag at C-terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

The Fractalkine solution (0.5 mg/ml) contains 10% Glycerol and Phosphate Buffered Saline (pH 7.4).

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
EFNA3 belongs to the ephrin (EPH) family. The ephrins and EPH-related receptors include thelargest subfamily of receptor protein-tyrosine kinases which have been implicated in mediating developmental events, especially in the nervous system and in erythropoiesis. Ephrins are divided into the ephrin-A (EFNA) class and the ephrin-B (EFNB) class, based on their structures and sequence relationships. The Ephrins from the EFNA class are anchored to the membrane by aglycosylphosphatidylinositol linkage, while the others from the EFNB class are transmembrane proteins.
Synonyms
Ephrin-A3, EFL2, Ehk1-L, EPLG3, LERK3, EPH-related receptor tyrosine kinase ligand 3.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
ADPQGPGGAL GNRHAVYWNS SNQHLRREGY TVQVNVNDYL DIYCPHYNSS GVGPGAGPGP
GGGAEQYVLY MVSRNGYRTC NASQGFKRWE CNRPHAPHSP IKFSEKFQRY SAFSLGYEFH
AGHEYYYIST PTHNLHWKCL RMKVFVCCAS TSHSGEKPVP TLPQFTMGPN VKINVLEDFE
GENPQVPKLE KSISGLEPKS CDKTHTCPPC PAPELLGGPS VFLFPPKPKD TLMISRTPEV
TCVVVDVSHE DPEVKFNWYV DGVEVHNAKT KPREEQYNST YRVVSVLTVL HQDWLNGKEY
KCKVSNKALP APIEKTISKA KGQPREPQVY TLPPSRDELT KNQVSLTCLV KGFYPSDIAV
EWESNGQPEN NYKTTPPVLD SDGSFFLYSK LTVDKSRWQQ GNVFSCSVMH EALHNHYTQK SLSLSPGKHH
HHHH

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.

Description:

Elamipretide

SS-31, MTP-131, Bendavia.

Product # :

HOR-040

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HPLC, MS

Description

Elamipretide Synthetic is a single, non-glycosylated polypeptide chain containing 4 amino acids, having a molecular mass of 639.79 Dalton and a Molecular formula of C32H49N9O5
.

Source

Synthetic Peptide

Formulation

The protein was lyophilized with no additives.

Purity

Greater than 97.0% as determined by analysis by RP-HPLC.

HPLC, MS

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Synonyms
SS-31, MTP-131, Bendavia.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Elamipretide although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Elamipretide should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Elamipretide in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
H-D-Arg-(2',6'-dimethyl-Tyr)-Lys-Phe-NH2
Background
What is the molecular weight/Mw of Elamipretide Protein?
Elamipretide Protein has a total Mw of 639Da.
What is the source or expression system of Elamipretide Protein?
Synthetic peptide

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

What is the Biological Activity of Elamipretide Protein?
The biological functionality of Elamipretide Protein will be determined in the future.

What is the amino acid sequence of Elamipretide Protein?
H-D-Arg-(2',6'-dimethyl-Tyr)-Lys-Phe-NH2

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

What is the endotoxin level for Elamipretide Protein?
The endotoxin level is minimal, Elamipretide Protein was purified using conventional chromatography techniques.
Elamipretide (also known as SS-31) is a novel mitochondrial-targeted peptide with immense promise as a therapeutic agent in mitochondrial dysfunction-related disorders. This research paper aims to provide a comprehensive analysis of Elamipretide, delving into its biochemical properties, mechanisms of action, and potential applications in various disease conditions.
Elamipretide, a mitochondria-targeting tetrapeptide, has garnered attention for its unique ability to protect mitochondria from oxidative stress and attenuate mitochondrial dysfunction (Siegel et al., 2013). This paper endeavors to explore Elamipretide's biochemical basis and its potential as a therapeutic agent in various diseases linked to mitochondrial impairment.
Elamipretide selectively accumulates within the inner mitochondrial membrane, where it exerts its cytoprotective effects. By reducing reactive oxygen species (ROS) production and enhancing electron transport chain efficiency, Elamipretide plays a crucial role in mitochondrial homeostasis (Kloner et al., 2015).
The mitochondrial protective actions of Elamipretide arise from its interaction with cardiolipin, a phospholipid predominantly localized in the inner mitochondrial membrane. By binding to cardiolipin, Elamipretide stabilizes mitochondrial cristae, improves membrane integrity, and enhances oxidative phosphorylation (Minkler et al., 2015).
Elamipretide's potential applications extend to a myriad of disease conditions characterized by mitochondrial dysfunction. In preclinical studies, Elamipretide has shown promise in mitigating tissue damage following ischemia-reperfusion injury, preserving cardiac function after myocardial infarction, and ameliorating neurodegenerative processes (Birk et al., 2017; Cho et al., 2015).
As the research on Elamipretide progresses, further investigation is warranted to better understand its pharmacokinetics, long-term safety, and potential off-target effects. Clinical trials exploring its therapeutic efficacy in human diseases offer exciting prospects for the future.
Elamipretide, a mitochondria-targeting peptide, emerges as a promising candidate in combating mitochondrial dysfunction-related disorders. Its unique ability to stabilize mitochondrial membranes and enhance cellular bioenergetics positions Elamipretide as a novel therapeutic option for a diverse range of diseases.

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.

Description:

Tirzepatide

Product # :

HOR-057

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Description

Tirzepatide is a synthetic single, non-glycosylated polypeptide chain containing 39 amino acids, having a molecular mass of 4813 Dalton and a Molecular formula of C187H291N45O59.

Formulation

The protein was lyophilized with no additives.

Purity

Greater than 97.0% as determined by analysis by RP-HPLC.

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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Tirzepatide although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Tirzepatide should be stored at 4°C between 2-7 days and for future use below -18°C.
For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Tirzepatide in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
His-Ala-Glu-Gly-Thr-Phe-Thr-Ser-Asp-Tyr-Ser-Ile-Aib-Leu-Asp-Lys-Ile-Ala-Gln-Lys (Eicosanedioyl-isoGlu-PEG2-PEG2)-Ala-Phe-Val-Gln-Trp-Leu-Ile-Ala-Gly-Gly-Pro-Ser-Ser-Gly-Ala-Pro-Pro-Pro-Ser-NH2.
Background
Tirzepatide is a first-in-class dual glucose-dependent insulinotropic polypeptide and glucagon-like peptide-1 receptor agonist. Recent development suggests Tirzepatide as organ protection and systemic metabolic health while at first, it was only approved for Type 2 Diabetes and Chronic Weight Management. Preclinical data also indicates a promising future in neuroprotection and most likely to expand its clinical utility into neurodegenerative pathologies.

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.

Description:

Epidermal Growth Factor Receptor Human Recombinant Sf9, Active

Epidermal growth factor receptor, EC 2.7.10.1, Receptor tyrosine-protein kinase ErbB-1, ERBB, mENA, ERBB1, EGFR.

Product # :

PKA-335

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Description

EGFR Human Recombinant encoding a.a. 672-1210 expressed in Baculovirus infected Sf9 cells, fused with a GST-tag at N-terminus with thrombin cleavage sites, having a molecular weight of 89,171 Dalton.EGFR is purified by proprietary chromatographic techniques.

Source

Baculovirus infected Sf9 cells.

Formulation

EGFR in 50mM HEPES pH 7.5, 100mM NaCl, 5mM DTT, 15mM reduced glutathione and 20% glycerol.

Biological Activity

Determination of Km value by Filter binding assay MAFC membrane.

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Introduction
The epidermal growth factor receptor (EGF R) subfamily of receptor tyrosine kinases comprises four members: EGF R (also known as HER1, ErbB1 or ErbB), ErbB2 (Neu, HER-2), ErbB3 (HER-3), and ErbB4 (HER-4). All family members are type I transmembrane glycoprotein that has an extracellular domain which contains two cysteine-rich domains separated by a spacer region that is involved in ligand-binding, and a cytoplasmic domain which has a membrane-proximal tyrosine kinase domain and a C-terminal tail with multiple tyrosine autophosphorylation sites. The human EGF R gene encodes a 1210 amino acid (aa) residue precursor with a 24 aa putative signal peptide, a 621 aa extracellular domain, a 23 aa transmembrane domain, and a 542 aa cytoplasmic domain. EGF R has been shown to bind a subset of the EGF family ligands, including EGF, amphiregulin, TGF-a , betacellulin, epiregulin, heparin-binding EGF and neuregulin-2 in the absence of a co-receptor. Ligand binding induces EGF R homodimerization as well as heterdimerization with ErbB2, resulting in kinase activation, tyrosine phosphorylation and cell signaling. EGF R can also be recruited to form heterodimers with the ligand-activated ErbB3 or ErbB4. EGF R signaling has been shown to regulate multiple biological functions including cell proliferation, differentiation, motility and apoptosis. In addition, EGF R signaling has also been shown to play a role in carcinogenesis.
Synonyms
Epidermal growth factor receptor, EC 2.7.10.1, Receptor tyrosine-protein kinase ErbB-1, ERBB, mENA, ERBB1, EGFR.
Physical Appearance
Sterile filtered liquid.
Stability
Store vial at -20°C to -80°C. When stored at the recommended temperature, this protein is stable for 12 months. Please avoid freeze-thaw cycles.
Specific Activity
30 pmol/µgxmin.

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.

Description:

Ephrin A1 Human Recombinant, Sf9

Ephrin A1, Immediate Early Response Protein B61, TNF Alpha-Induced Protein 4, Ephrin-A1, TNFAIP4, LERK-1, EPLG1, LERK1, Tumor Necrosis Factor, Alpha-Induced Protein 4, Eph-Related Receptor Tyrosine Kinase Ligand 1, EPH-Related Receptor Tyrosine Kinase Ligand 1, Tumor Necrosis Factor Alpha-Induced Protein 4, Ligand Of Eph-Related Kinase 1, ECKLG, EFL1, B61, EPH-related receptor tyrosine kinase ligand 1, LERK-1.

Product # :

PRO-2538

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Description

EFNA1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 406 amino acids (19-182a.a.) and having a molecular mass of 46.6kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).EFNA1 is expressed with a 242 amino acid hIgG-His-tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

EFNA1 protein solution (0.5mg/ml) contains 10% glycerol & Phosphate Buffered Saline (pH 7.4).

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
EFNA1 belongs to the ephrin (EPH) family. The EPH subfamily is the biggest group of receptor protein kinases and they take part in vital nervous system function and development.
Synonyms
Ephrin A1, Immediate Early Response Protein B61, TNF Alpha-Induced Protein 4, Ephrin-A1, TNFAIP4, LERK-1, EPLG1, LERK1, Tumor Necrosis Factor, Alpha-Induced Protein 4, Eph-Related Receptor Tyrosine Kinase Ligand 1, EPH-Related Receptor Tyrosine Kinase Ligand 1, Tumor Necrosis Factor Alpha-Induced Protein 4, Ligand Of Eph-Related Kinase 1, ECKLG, EFL1, B61, EPH-related receptor tyrosine kinase ligand 1, LERK-1.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
ADPDRHTVFW NSSNPKFRNE DYTIHVQLND YVDIICPHYE DHSVADAAME QYILYLVEHE EYQLCQPQSK DQVRWQCNRP SAKHGPEKLS EKFQRFTPFT LGKEFKEGHS YYYISKPIHQ HEDRCLRLKV TVSGKITHSP QAHVNPQEKR LAADDPEVRV LHSIGHSLEP KSCDKTHTCP PCPAPELLGG PSVFLFPPKP KDTLMISRTP EVTCVVVDVS HEDPEVKFNW YVDGVEVHNA KTKPREEQYN STYRVVSVLT VLHQDWLNGK EYKCKVSNKA LPAPIEKTIS KAKGQPREPQ VYTLPPSRDE LTKNQVSLTC LVKGFYPSDI AVEWESNGQP ENNYKTTPPV LDSDGSFFLY SKLTVDKSRW QQGNVFSCSV MHEALHNHYT QKSLSLSPGK 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.

Description:

Ephrin- B2 Human Recombinant

Ephrin-B2, EPH-related receptor tyrosine kinase ligand 5, LERK-5, HTK ligand, HTK-L, EFNB2, EPLG5, HTKL, LERK5, MGC126226, MGC126227, MGC126228.

Product # :

PRO-937

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Description

EFNB2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 227 amino acids (28-229 a.a.) and having a molecular mass of 24.9kDa.EFNB2 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

EFNB2 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 20% glycerol and 200mM NaCl.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
Ephrin-B2 belongs to the ephrin (EPH) family. The ephrins and EPH-related receptors contain the largest subfamily of receptor protein-tyrosine kinases and have been associated with mediating developmental events, particularly in the nervous system and in erythropoiesis. Based upon their structures and sequence relationships, ephrins are allocated into the ephrin-A (EFNA) class, which are anchored to the membrane by a glycosylphosphatidylinositol linkage, and the ephrin-B (EFNB) class, which are transmembrane proteins. Ephrin-B2 binds to the EPHB4 and EPHA3 receptors.
Synonyms
Ephrin-B2, EPH-related receptor tyrosine kinase ligand 5, LERK-5, HTK ligand, HTK-L, EFNB2, EPLG5, HTKL, LERK5, MGC126226, MGC126227, MGC126228.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMIVLEP IYWNSSNSKF LPGQGLVLYP QIGDKLDIIC PKVDSKTVGQ YEYYKVYMVD KDQADRCTIK KENTPLLNCA KPDQDIKFTI KFQEFSPNLW GLEFQKNKDY YIISTSNGSL EGLDNQEGGV CQTRAMKILM KVGQDASSAG STRNKDPTRR PELEAGTNGR SSTTSPFVKP NPGSSTDGNS AGHSGNNILG SEVALFA.

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Description:

Eukaryotic Translation Initiation Factor 1 X-linked Human Recombinant

eukaryotic translation initiation factor 1A, X-linked, eIF-4C, EIF1A, EIF4C, eIF-1A, EIF1AP1.

Product # :

PRO-253

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Description

EIF1AX Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 150 amino acids (1-144a.a.) and having a molecular wieght of 18.6kDa. EIF1AX is fused to 20a.a. His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The EIF1AX protein solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH8.0) containing 5mM DTT, 200mM NaCl and 40% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
EIF1AX is an important eukaryotic translation initiation factor. EIF1AX is essential for the binding of the 43S complex (a 40S subunit, eIF2/GTP/Met-tRNAi and eIF3) to the 5'' end of capped RNA. EIF1AP1 is needed for maximal rate of protein biosynthesis. EIF1AX increases ribosome dissociation into subunits and stabilizes the binding of the initiator Met-tRNA (I) to 40 S ribosomal subunits.
Synonyms
eukaryotic translation initiation factor 1A, X-linked, eIF-4C, EIF1A, EIF4C, eIF-1A, EIF1AP1.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MPKNKGKGGK NRRRGKNENE SEKRELVFKE DGQEYAQVIK MLGNGRLEAM CFDGVKRLCH IRGKLRKKVW INTSDIILVG LRDYQDNKAD VILKYNADEA RSLKAYGELP EHAKINETDT FGPGDDDEIQ FDDIGDDDED IDDI

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Description:

Eukaryotic Translation Initiation Factor 1B Human Recombinant

Eukaryotic translation initiation factor 1b, eIF1b, Protein translation factor SUI1 homolog GC20, EIF1B, GC20.

Product # :

PRO-175

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Description

EIF1B 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 133 amino acids (1-113 a.a.) and having a molecular mass of 15kDa. The EIF1B is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The EIF1B solution (1 mg/ml) contains 20mM Tris-HCl buffer(pH 8.0), 10% glycerol, 2mM DTT and 0.1M NaCl.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
EIF1B is critical for the scanning process in vitro. EIF1B is an element of a complex involved in recognition of the initiator codon during the scanning process. Translation is also initiated by the function of EIF1B in regulating the activity of ribosomal subunits 43S, 48S and 40S. EIF1B enables 43S ribosomal complexes to distinguish between cognate and near-cognate initiation codons, perceiving the nucleotide content of initiation codons.
Synonyms
Eukaryotic translation initiation factor 1b, eIF1b, Protein translation factor SUI1 homolog GC20, EIF1B, GC20.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSTIQNLQSF DPFADATKGD DLLPAGTEDY IHIRIQQRNG RKTLTTVQGI ADDYDKKKLV KAFKKKFACN GTVIEHPEYG EVIQLQGDQR KNICQFLLEV GIVKEEQLKV HGF.

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.

Description:

ER Membrane Protein Complex Subunit 2 Human Recombinant

ER Membrane Protein Complex Subunit 2, KIAA0103, Tetratricopeptide Repeat Domain 35, Tetratricopeptide Repeat Protein 35, TPR Repeat Protein 35, TTC35.

Product # :

PRO-1613

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Description

EMC2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 320 amino acids (1-297) and having a molecular mass of 37.2kDa.EMC2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The EMC2 solution contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 2mM DTT and 40% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
EMC2 is an element of the ER membrane protein complex. EMC2 is a member of the EMC2 family and holds 3 TPR repeats.
Synonyms
ER Membrane Protein Complex Subunit 2, KIAA0103, Tetratricopeptide Repeat Domain 35, Tetratricopeptide Repeat Protein 35, TPR Repeat Protein 35, TTC35.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAKVSEL YDVTWEEMRD KMRKWREENS RNSEQIVEVG EELINEYASK LGDDIWIIYE QVMIAALDYG RDDLALFCLQ ELRRQFPGSH RVKRLTGMRF EAMERYDDAI QLYDRILQED PTNTAARKRK IAIRKAQGKN VEAIRELNEY LEQFVGDQEA WHELAELYIN EHDYAKAAFC LEELMMTNPH NHLYCQQYAE VKYTQGGLEN LELSRKYFAQ ALKLNNRNMR ALFGLYMSAS HIASNPKASA KTKKDNMKYA SWAASQINRA YQFAGRSKKE TKYSLKAVED MLETLQITQS.

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Description:

Excision Repair Cross-Complementing 1 Human Recombinant

Excision Repair Cross-complementing rodent repair deficiency complementation group 1 (includes overlapping antisense sequence), RAD10, COFS4, UV20, DNA excision repair protein ERCC-1.

Product # :

PRO-1106

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Description

ERCC1 Human Recombinant produced in E. coli is a single polypeptide chain containing 297 amino acids (1-273) and having a molecular mass of 32.5kDa.ERCC1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The ERCC1 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 1mM DTT and 20% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
ERCC1 polypeptide is essential for nucleotide excision repair (NER) of damaged DNA and is homologous to Saccharomyces cerevisiae RAD10, which takes part in repair and mitotic intra-chromosomal recombination. NER mechanism includes dual incisions on both sides of the damage catalyzed by two nucleases. In mammalian cells XPG cleaves 3' of the DNA lesion while the ERCC1-XPF complex makes the 5' incision.
Synonyms
Excision Repair Cross-complementing rodent repair deficiency complementation group 1 (includes overlapping antisense sequence), RAD10, COFS4, UV20, DNA excision repair protein ERCC-1.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMDPGKD KEGVPQPSGP PARKKFVIPL DEDEVPPGVA KPLFRSTQSL PTVDTSAQAA PQTYAEYAIS QPLEGAGATC PTGSEPLAGE TPNQALKPGA KSNSIIVSPR QRGNPVLKFV RNVPWEFGDV IPDYVLGQST CALFLSLRYH NLHPDYIHGR LQSLGKNFAL RVLLVQVDVK DPQQALKELA KMCILADCTL ILAWSPEEAG RYLETYKAYE QKPADLLMEK LEQDFVSRSL EQLIAASRED LALCPGLGPQ KARRLFDVLH EPFLKVP

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.

Description:

Natriuretic Peptide A Human Recombinant

Natriuretic peptides A, CDD-ANF, Cardiodilatin, CDD, Cardiodilatin-related peptide, CDP, N-terminal proatrial natriuretic peptide, ANP, PND.

Product # :

CYT-1028

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Description

NPPA Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 26-123) containing 106 amino acids including an 8 a.a N-terminal His tag. The total molecular mass is 11.7kDa (calculated).

Source

Escherichia Coli.

Formulation

NPPA filtered (0.4 µm) and lyophilized from 0.5mg/ml in 20 mM Tris buffer, 50 mM NaCl and 5% w/v trehalosa, pH 7.5.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Natriuretic Peptide A (NPPA) is a part of the natriuretic peptide family and is involved in cardiovascular homeostasis through regulation of natriuresis, diuresis, and vasodilation. NPPA is synthesized as a great precursor which releases a peptide from the N-terminus with similarity to vasoactive peptide, cardiodilatin, and another peptide from the C-terminus with natriuretic-diuretic activity. In female pregnancy, NPPA is promoting trophoblast invasion and spiral artery remodeling in uterus.
Synonyms
Natriuretic peptides A, CDD-ANF, Cardiodilatin, CDD, Cardiodilatin-related peptide, CDP, N-terminal proatrial natriuretic peptide, ANP, PND.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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.
Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. NPPA is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
Amino Acid Sequence
MKHHHHHHNP MYNAVSNADL MDFKNLLDHL EEKMPLEDEV VPPQVLSEPN EEAGAALSPL PEVPPWTGEV SPAQRDGGAL GRGPWDSSDR SALLKSKLRA LLTAPR.

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.

Description:

Rho GDP Dissociation Inhibitor (GDI) Beta Human Recombinant

Rho GDP dissociation inhibitor (GDI) beta, Rho GDI 2, Rho-GDI beta, GDIA2, GDID4, Ly-GDI, RAP1GN1.

Product # :

PRO-1067

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Description

ARHGDIB Human Recombinant produced in E. coli is a single polypeptide chain containing 428 amino acids (1-201) and having a molecular mass of 49.4kDa.ARHGDIB is fused to a 227 amino acid GST-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The ARHGDIB solution (1mg/1ml) contains phosphate-buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Members of the Rho (or ARH) protein family and other Ras-related small GTP-binding proteins are involved in various cellular procedures, such as cell cytoskeletal organization, secretion, proliferation, and signaling. The GTPBPs are active only in the GTP-bound state. At least 3 types of proteins firmly regulate cycling between the GTP-bound and GDP-bound states: GDP-dissociation inhibitors (GDIs), GTPase-activating proteins (GAPs) and guanine nucleotide-releasing factors (GRFs). ARHGDIB and the other GDIs lower the level of GDP dissociation from Ras-like GTPases.
Synonyms
Rho GDP dissociation inhibitor (GDI) beta, Rho GDI 2, Rho-GDI beta, GDIA2, GDID4, Ly-GDI, RAP1GN1.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MSPILGYWKI KGLVQPTRLL LEYLEEKYEE HLYERDEGDK WRNKKFELGL EFPNLPYYID GDVKLTQSMA IIRYIADKHN MLGGCPKERA EISMLEGAVL DIRYGVSRIA YSKDFETLKV DFLSKLPEML KMFEDRLCHK TYLNGDHVTH PDFMLYDALD VVLYMDPMCL DAFPKLVCFK KRIEAIPQID KYLKSSKYIA WPLQGWQATF GGGDHPPKSD LVPRGSHMTE KAPEPHVEED DDDELDSKLN YKPPPQKSLK ELQEMDKDDE SLIKYKKTLL GDGPVVTDPK APNVVVTRLT LVCESAPGPI TMDLTGDLEA LKKETIVLKE GSEYRVKIHF KVNRDIVSGL KYVQHTYRTG VKVDKATFMV GSYGPRPEEY EFLTPVEEAP KGMLARGTYH NKSFFTDDDK QDHLSWEWNL SIKKEWTE

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.

Description:

Angiopoietin-like Protein 2 Human Recombinant

Angiopoietin-related protein 2, Angiopoietin-like protein 2, ANGPTL2, ARP2, HARP.

Product # :

CYT-765

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Description

ANGPTL2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 493 amino acids ( 22-493 a.a.) including a 20 a.a N-terminal His tag. The total molecular mass is 57.1kDa (calculated).

Source

Escherichia Coli.

Formulation

ANGPTL2 protein solution (0.5mg/ml) contains 20mM Tris HCL (pH7-8) and 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
Angiopoietins belong to the vascular endothelial growth factor family and the only known growth factors largely specific for vascular endothelium. Angiopoietins-1, 2 and 4 partake in the formation of blood vessels. ANGPTL2 displays angiogenic effects. Angiopoietin-like Protein 2 (ANGPTL2) is an anti-diabetic factor. ANGPTL2 induces sprouting in endothelial cells through an autocrine and paracrine action. ANGPTL2 increases insulin sensitivity in adipocytes. In addition, ANGPTL2 is a mediator of chronic adipose tissue inflammation. ANGPTL2 is widely expressed in the heart, small intestine, spleen and stomach. ANGPTL2 is also found in lower levels in the colon, ovary, adrenal gland, skeletal muscle and in prostate.
Synonyms
Angiopoietin-related protein 2, Angiopoietin-like protein 2, ANGPTL2, ARP2, HARP.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGQEDGFEGT EEGSPREFIY LNRYKRAGES QDKCTYTFIV PQQRVTGAIC VNSKEPEVLL ENRVHKQELE LLNNELLKQK RQIETLQQLV EVDGGIVSEV KLLRKESRNM NSRVTQLYMQ LLHEIIRKRD NALELSQLEN RILNQTADML QLASKYKDLE HKYQHLATLA HNQSEIIAQL EEHCQRVPSA RPVPQPPPAA PPRVYQPPTY NRIINQISTN EIQSDQNLKV LPPPLPTMPT LTSLPSSTDK PSGPWRDCLQ ALEDGHDTSS IYLVKPENTN RLMQVWCDQR HDPGGWTVIQ RRLDGSVNFF RNWETYKQGF GNIDGEYWLG LENIYWLTNQ GNYKLLVTME DWSGRKVFAE YASFRLEPES EYYKLRLGRY HGNAGDSFTW HNGKQFTTLD RDHDVYTGNC AHYQKGGWWY NACAHSNLNG VWYRGGHYRS RYQDGVYWAE FRGGSYSLKK VVMMIRPNPN TFH
Background
Angiopoietin-like Protein 2 Human Recombinant: A Potential Therapeutic Target for Metabolic and Cardiovascular Disorders
Abstract:
Angiopoietin-like protein 2 (ANGPTL2) has emerged as a crucial regulator in metabolic and cardiovascular disorders. This multifunctional protein is involved in various biological processes, including angiogenesis, adipose tissue function, and inflammation. The availability of human recombinant ANGPTL2 protein has provided researchers with a valuable tool to explore its therapeutic potential. This concise review provides an overview of the role of ANGPTL2 in metabolic and cardiovascular health and discusses the potential of ANGPTL2 human recombinant protein as a therapeutic target.
Introduction:
Metabolic disorders, such as obesity and type 2 diabetes, are closely associated with cardiovascular diseases and pose significant global health challenges. ANGPTL2, a member of the angiopoietin-like protein family, has gained attention for its involvement in metabolic regulation and cardiovascular homeostasis. Through interactions with various receptors and signaling pathways, ANGPTL2 influences lipid metabolism, insulin sensitivity, inflammation, and vascular integrity.
Mechanisms of ANGPTL2 Action:
ANGPTL2 acts through binding to integrins, toll-like receptors (TLRs), and other receptors on different cell types, including adipocytes, endothelial cells, and immune cells. By influencing angiogenesis, inflammation, and extracellular matrix remodeling, ANGPTL2 affects adipose tissue function, lipid metabolism, and insulin signaling.
Role of ANGPTL2 in Metabolic Regulation:
ANGPTL2 plays a critical role in metabolic regulation and the development of metabolic disorders. It promotes adipose tissue inflammation, impairs adipogenesis, and alters adipokine secretion, contributing to metabolic dysfunction. Furthermore, ANGPTL2 modulates lipid metabolism by regulating lipoprotein lipase activity, affecting triglyceride clearance, and promoting hepatic lipid accumulation.
ANGPTL2 in Cardiovascular Health and Disease:
Increasing evidence suggests that ANGPTL2 is implicated in cardiovascular diseases, including atherosclerosis and heart failure. ANGPTL2 promotes vascular inflammation, endothelial dysfunction, and smooth muscle cell proliferation, which contribute to atherosclerotic plaque progression and vascular remodeling. Additionally, ANGPTL2 influences cardiac remodeling and fibrosis, impacting heart failure development.
Therapeutic Potential of ANGPTL2 Human Recombinant Protein:
The availability of ANGPTL2 human recombinant protein opens avenues for therapeutic interventions targeting metabolic and cardiovascular disorders. Preclinical studies employing ANGPTL2 blockade or supplementation have shown promising results in improving metabolic parameters, reducing atherosclerosis, and preserving cardiac function. However, further research is needed to optimize the clinical application of ANGPTL2 human recombinant protein, including dosage, timing, and delivery methods.
Conclusion:
ANGPTL2 holds promise as a therapeutic target for metabolic and cardiovascular disorders. Its involvement in key biological processes makes it an attractive candidate for interventions aiming to improve metabolic health and prevent cardiovascular complications. The development of ANGPTL2 human recombinant protein provides a valuable tool for investigating its therapeutic potential further.
What is the molecular weight/Mw of ANGPTL2 Protein?
ANGPTL2 Protein has a total Mw of 57.1kDa.

What is the source or expression system of ANGPTL2 Protein?
Escherichia Coli.

What is the Purity of ANGPTL2 Protein?
ANGPTL2 Protein is >85% pure as determined by SDS-PAGE.

What is the Biological Activity of ANGPTL2 Protein?
The biological functionality of ANGPTL2 Protein will be determined in the future.

What is the amino acid sequence of ANGPTL2 Protein?
MGSSHHHHHH SSGLVPRGSH MGQEDGFEGT EEGSPREFIY LNRYKRAGES QDKCTYTFIV PQQRVTGAIC VNSKEPEVLL ENRVHKQELE LLNNELLKQK RQIETLQQLV EVDGGIVSEV KLLRKESRNM NSRVTQLYMQ LLHEIIRKRD NALELSQLEN RILNQTADML QLASKYKDLE HKYQHLATLA HNQSEIIAQL EEHCQRVPSA RPVPQPPPAA PPRVYQPPTY NRIINQISTN EIQSDQNLKV LPPPLPTMPT LTSLPSSTDK PSGPWRDCLQ ALEDGHDTSS IYLVKPENTN RLMQVWCDQR HDPGGWTVIQ RRLDGSVNFF RNWETYKQGF GNIDGEYWLG LENIYWLTNQ GNYKLLVTME DWSGRKVFAE YASFRLEPES EYYKLRLGRY HGNAGDSFTW HNGKQFTTLD RDHDVYTGNC AHYQKGGWWY NACAHSNLNG VWYRGGHYRS RYQDGVYWAE FRGGSYSLKK VVMMIRPNPN TFH

What applications can ANGPTL2 Protein be used in?
ANGPTL2 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for ANGPTL2 Protein?
The endotoxin level is minimal, ANGPTL2 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.

Description:

Proheparin-Binding EGF-like Growth Factor Rat Recombinant

Proheparin-binding EGF-like growth factor, Heparin-binding EGF-like growth factor, HB-EGF, HBEGF, Dtr, Hegfl, GFHB.

Product # :

CYT-170

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Description

HB-EGF Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 86 amino acids and having a molecular mass of 9.7kDa.The HB-EGF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was filtered (0.2µm) and lyophilized from a concentrated solution containing PBS, 300mM NaCl, pH 7.4 and 5% trehalose.

Purity

Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The ED₅₀ as determined by a cell proliferation assay using balb/c 3T3 cells is < 1.0 ng/ml, corresponding to a specific activity of > 1.0×10⁶ units/mg.

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Introduction
HB-EGF is an EGF related growth factor which signals via the EGF receptor, and stimulates the proliferation of SMC (smooth muscle cells), fibroblasts, epithelial cells and keratinocytes. HB-EGF is expressed in various cell types and tissues, including vascular endothelial cells and SMC, macrophages, skeletal muscle, keratinocytes and particular tumor cells. HB-EGF’s ability to explicitly bind heparin and heparin sulfate proteoglycans is dissimilar from other EGF-like molecules, and might be related to the enhanced mitogenic activity, relative to EGF, that HB-EGF exerts on smooth muscle cells.
Synonyms
Proheparin-binding EGF-like growth factor, Heparin-binding EGF-like growth factor, HB-EGF, HBEGF, Dtr, Hegfl, GFHB.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Rat HB-EGF Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution HB-EGF should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Rat HB-EGF in sterile 18M-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
DLEGTDLDLF KVAFSSKPQA LATPGKEKNG KKKRKGKGLG KKRDPCLKKY KDYCIHGECR YLKELRIPSC HCLPGYHGQR CHGLTL.
Background
What is the molecular weight/Mw of HB-EGF Protein?
HB-EGF Protein has a total Mw of 9.7kDa.

What is the source or expression system of HB-EGF Protein?
Escherichia Coli.

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

What is the Biological Activity of HB-EGF Protein?
The ED50 as determined by a cell proliferation assay using balb/c 3T3 cells is < 1.0 ng/ml, corresponding to a specific activity of > 1.0×106 units/mg.

What is the amino acid sequence of HB-EGF Protein?
DLEGTDLDLF KVAFSSKPQA LATPGKEKNG KKKRKGKGLG KKRDPCLKKY KDYCIHGECR YLKELRIPSC HCLPGYHGQR CHGLTL.

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

What is the endotoxin level for HB-EGF Protein?
The endotoxin level is minimal, HB-EGF 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.

Description:

Angiopoietin 2 Human Recombinant

Angiopoietin-2, Angiopoietin2, ANGPT2, ANG2, ANG-2, ANGPT-2.

Product # :

CYT-1103

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Description

ANGPT2 produced in Chinese hamster ovary (CHO) cells by recombinant DNA technology is a single, polypeptide chain (19-496 a.a.) and fused to a 6 aa His Tag at C-terminus containing a total of 484 amino acids and having a molecular mass of 55.7kDa.ANGPT2 shows multiple bands between 50-100kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.

Source

Chinese Hamster Ovary Cells (CHO).

Formulation

ANGPT2 protein solution (0.25mg/ml) contains Phosphate buffered saline (pH7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
ANGPT2 aka Angiopoietin-2 competes for binding to the TIE2 receptor and blocks angiopoietin-1 aka ANGPT1 induced TIE2 autophosphorylation during vasculogenesis. ANGPT-2 is a naturally occurring antagonist of ANGPT-1. ANGPT2 induces tyrosine phosphorylation of TEK/TIE2 in the lack of Angiopoietin-2. In the deficiency of VEGF an angiogenic inducer, ANGPT-2 induces endothelial cell apoptosis resulting in vascular regression. ANGPT2 along with VEGF enable endothelial cell migration and proliferation, resulting in permissive angiogenic signal.
Synonyms
Angiopoietin-2, Angiopoietin2, ANGPT2, ANG2, ANG-2, ANGPT-2.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
YNNFRKSMDS IGKKQYQVQH GSCSYTFLLP EMDNCRSSSS PYVSNAVQRD APLEYDDSVQ
RLQVLENIME NNTQWLMKLE NYIQDNMKKEMVEIQQNAVQ NQTAVMIEIG TNLLNQTAEQ
TRKLTDVEAQ VLNQTTRLEL QLLEHSLSTN KLEKQILDQT SEINKLQDKN
SFLEKKVLAMEDKHIIQLQS IKEEKDQLQV LVSKQNSIIE ELEKKIVTAT VNNSVLQKQQ
HDLMETVNNL LTMMSTSNSA KDPTVAKEEQ ISFRDCAEVFKSGHTTNGIY TLTFPNSTEE
IKAYCDMEAG GGGWTIIQRR EDGSVDFQRT WKEYKVGFGN PSGEYWLGNE FVSQLTNQQR
YVLKIHLKDWEGNEAYSLYE HFYLSSEELN YRIHLKGLTG TAGKISSISQ PGNDFSTKDG
DNDKCICKCS QMLTGGWWFD ACGPSNLNGM YYPQRQNTNKFNGIKWYYWK GSGYSLKATT MMIRPADFHH HHHH
Background
6. Therapeutic Implications of Ang-2
Given its critical role in angiogenesis and its involvement in various disease states, Ang-2 represents a promising target for therapeutic interventions. Strategies aimed at modulating Ang-2 signaling, such as the development of neutralizing antibodies or small molecule inhibitors, hold great potential for managing angiogenesis-related disorders and improving patient outcomes.
7. Conclusion and Future Perspectives
Our understanding of Ang-2 and its multifaceted involvement in angiogenesis has advanced significantly. However, further research is required to elucidate the complex interplay between Ang-2 and other angiogenic factors, as well as to explore the potential of Ang-2-targeted therapies. Continued investigations will pave the way for the development of innovative treatment approaches for angiogenesis-related disorders, ultimately improving patient care.
What is the molecular weight/Mw of ANGPT2 Protein?
ANGPT2 Protein has a total Mw of 55.7kDa.

What is the source or expression system of ANGPT2 Protein?
Chinese Hamster Ovary Cells

What is the Purity of ANGPT2 Protein?
ANGPT2 Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of ANGPT2 Protein?
The biological functionality of ANGPT2 Protein will be determined in the future.

What is the amino acid sequence of ANGPT2 Protein?
YNNFRKSMDS IGKKQYQVQH GSCSYTFLLP EMDNCRSSSS PYVSNAVQRD APLEYDDSVQ
RLQVLENIME NNTQWLMKLE NYIQDNMKKEMVEIQQNAVQ NQTAVMIEIG TNLLNQTAEQ
TRKLTDVEAQ VLNQTTRLEL QLLEHSLSTN KLEKQILDQT SEINKLQDKN
SFLEKKVLAMEDKHIIQLQS IKEEKDQLQV LVSKQNSIIE ELEKKIVTAT VNNSVLQKQQ
HDLMETVNNL LTMMSTSNSA KDPTVAKEEQ ISFRDCAEVFKSGHTTNGIY TLTFPNSTEE
IKAYCDMEAG GGGWTIIQRR EDGSVDFQRT WKEYKVGFGN PSGEYWLGNE FVSQLTNQQR
YVLKIHLKDWEGNEAYSLYE HFYLSSEELN YRIHLKGLTG TAGKISSISQ PGNDFSTKDG
DNDKCICKCS QMLTGGWWFD ACGPSNLNGM YYPQRQNTNKFNGIKWYYWK GSGYSLKATT MMIRPADFHH HHHH

What applications can ANGPT2 Protein be used in?
ANGPT2 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for ANGPT2 Protein?
The endotoxin level is minimal, ANGPT2 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.

Description:

Epidermal Growth Factor (1-51 a.a.)Human Recombinant

Urogastrone, URG, EGF.

Product # :

CYT-1115

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Description

Epidermal Growth Factor (1-51 a.a.) Human Recombinant produced in yeast is a single, glycosylated polypeptide chain containing 51 amino acids and having a molecular mass of 6.0kDa. The EGF 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 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The ED50 is determined by a cell proliferation assay using murine Balb/c 3T3 cells and is < than 0.1 ng/ml, corresponding to a specific activity of > 1.0 × 10⁷ IU/mg.

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Introduction
Epidermal growth factor has a profound effect on the differentiation of specific cells in vivo and is a potent mitogenic factor for a variety of cultured cells of both ectodermal and mesodermal origin. The EGF precursor is believed to exist as a membrane-bound molecule which is proteolytically cleaved to generate the 53-amino acid peptide hormone that stimulates cells to divide. EGF stimulates the growth of several epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture.
Synonyms
Urogastrone, URG, EGF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized EGF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Epidermal Growth Factor should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Epidermal Growth Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
NSDSECPLSH DGYCLHDGVC MYIEALDKYA CNCVVGYIGE RCQYRDLKWW E.
Background
Exploring the Potential of Epidermal Growth Factor (1-51 a.a.) Human Recombinant: Novel Insights and Therapeutic Prospects
Abstract:
Epidermal Growth Factor (EGF) stands as a pivotal cytokine orchestrating essential cellular processes. This concise research paper delves into the unique realm of Epidermal Growth Factor (1-51 a.a.) Human Recombinant, unveiling its intricate molecular dynamics, signaling cascades, and therapeutic promise. Employing cutting-edge methodologies encompassing in vitro assays and animal models, this study elucidates the multifaceted cellular responses sparked by this truncated EGF variant, paving the way for potential clinical applications.
Introduction:
The truncated form of EGF, spanning amino acids 1 to 51 (a.a.), carries distinct attributes that set it apart from the full-length counterpart. This paper centers on exploring the intriguing dimensions of Epidermal Growth Factor (1-51 a.a.) Human Recombinant, offering new insights into its interactions and potential utility.
Molecular Insights and Signaling Dynamics:
At the heart of its function lies the interplay between EGF (1-51 a.a.) and the epidermal growth factor receptor (EGFR). High-resolution structural analyses unveil the nuances of their binding interface, initiating a cascade of phosphorylation events that trigger canonical and non-canonical signaling pathways. The MAPK pathway and the PI3K/Akt pathway, intricately modulated by EGF (1-51 a.a.), propel cellular processes like proliferation, migration, and evasion of apoptosis.
In Vitro Profiling and Cellular Responses:
In dissecting the cellular responses, diverse in vitro assays have been employed. These encompass cell viability assays, wound healing assays, and intricate fluorescence resonance energy transfer (FRET) studies. These assays converge to illuminate the dynamic orchestration of EGF-induced cellular behaviors, showcasing its role in promoting cellular migration, division, and wound closure.
In Vivo Implications and Therapeutic Horizons:
Translating these insights into tangible therapeutic possibilities, in vivo studies present a compelling narrative. In animal models, EGF (1-51 a.a.) emerges as a potent player in cutaneous wound healing, fostering accelerated tissue regeneration. Moreover, its potential extends to oncology, as it not only influences tumor microenvironments but also demonstrates anti-apoptotic effects, hinting at its role in tailored cancer interventions.
Future Prospects and Challenges:
While these discoveries hold immense promise, challenges persist. The intricate network of signaling events demands further scrutiny, considering potential cross-talk and off-target effects. Refining delivery mechanisms and dosing regimens is essential for realizing the clinical potential of EGF (1-51 a.a.).
Conclusion:
In a synthesis of complex molecular insights and tangible therapeutic potential, Epidermal Growth Factor (1-51 a.a.) Human Recombinant emerges as a captivating subject. Its truncated structure and distinctive signaling cascades paint a canvas of cellular orchestration. As research advances, harnessing its therapeutic benefits could usher in novel interventions for wound healing and cancer therapy.
What is the molecular weight/Mw of EGF Protein?
EGF Protein has a total Mw of 6kDa.

What is the source or expression system of EGF Protein?
Saccharomyces cerevisiae

What is the Purity of EGF Protein?
EGF Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of EGF Protein?
The ED50 is determined by a cell proliferation assay using murine Balb/c 3T3 cells and is < than 0.1 ng/ml, corresponding to a specific activity of > 1.0 × 107 IU/mg.

What is the amino acid sequence of EGF Protein?
NSDSECPLSH DGYCLHDGVC MYIEALDKYA CNCVVGYIGE RCQYRDLKWW E.

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

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

Description:

Enhanced Green Fluorescent Protein Recombinant

Green fluorescent protein, GFP.

Product # :

PRO-1606

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Description

Recombinant EGFP produced in E.coli cells is a single non-glycosylated protein containing 239 amino acid chain and having a molecular mass of 26.9kDa. EGFP is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The EGFP was 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.

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Introduction
GFP, also known as Green Fluorescent Protein, is a protein produced by the jellyfish (Aequorea Victoria) that produces bioluminescence in the green zone of the noticeable spectrum. Green Fluorescent Protein is a useful and ubiquitous instrument for producing chimeric proteins, where it functions as a fluorescent protein tag. GFP is expressed in most known cell types and is used as a noninvasive fluorescent marker in living cells and organisms. Green Fluorescent Protein permits a broad range of applications where it has functioned as a cell lineage tracer, reporter of gene expression, or as a measure of protein-protein interactions. Enhanced GFP (eGFP) has F64L and S65T mutations, which make GFP show increased fluorescence and fold more efficiently under 370.
Synonyms
Green fluorescent protein, GFP.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized EGFP although stable at room temperature for 3 weeks, should be stored desiccated below -180C. Upon reconstitution EGFP should be stored at 40C between 2-7 days and for future use below -180C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized EGFP in sterile distilled H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MVSKGEELFT GVVPILVELD GDVNGHKFSV SGEGEGDATY GKLTLKFICT TGKLPVPWPT LVTTLTYGVQ CFSRYPDHMK QHDFFKSAMP EGYVQERTIF FKDDGNYKTR AEVKFEGDTL VNRIELKGID FKEDGNILGH KLEYNYNSHN VYIMADKQKN GIKVNFKIRH NIEDGSVQLA DHYQQNTPIG DGPVLLPDNH YLSTQSALSK DPNEKRDHMV LLEFVTAAGI TLGMDELYK

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.

Description:

Thymosin β4

Thymosin beta-4. TB500, TB-500

Product # :

HOR-275

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

Thymosin b4 is a 43 amino acid peptide which is regarded as the main intracellular G-actin sequestering peptide. It has a molecular weight of 4963.55 Da, and its molecular formula is: C212H350N56O78S1. Extracellular Thymosin b4 may contribute to physiological processes such as angiogenesis, wound healing, and regulation of inflammation.

Formulation

The protein (1mg/ml) was lyophilized with no additives.

Purity

Greater than 98.0% as determined by RP-HPLC.

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Introduction
Thymosin is a hormone secreted from the thymus. Its primary function is to stimulate the production of T cells, which are an important part of the immune system. Thymosin also assists in the development of B cells to plasma cells to produce antibodies. The predominant form of thymosin, thymosin b4, is a member of a highly conserved family of actin monomer-sequestering proteins. b-thymosins are the primary regulators of unpolymerized actin, and are essential for maintaining the small cytoplasmic pool of free G-actin monomers required for rapid filament elongation and allowing for the flux of monomers between the thymosin-bound pool and F-actin.
Synonyms
Thymosin beta-4. TB500, TB-500
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Thymosin b4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution T beta 4 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Thymosin beta-4 in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
Thymosin b4 has an a.a. sequence of Ac-Ser-Asp-Lys-Pro-Asp-Met-Ala-Glu-Ile-Glu-Lys-Phe-Asp-Lys-Ser-Lys-Leu-Lys-Lys-Thr-Glu-Thr-Gln-Glu-Lys-Asn-Pro-Leu-Pro-Ser-Lys-Glu-Thr-Ile-Glu-Gln-Glu-Lys-Gln-Ala-Gly-Glu-Ser-OH.

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.

Description:

Elcatonin

Product # :

HOR-302

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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formulation
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biological activity
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Description

Elcatonin Synthetic is a single, non-glycosylated polypeptide chain containing 31 amino acids, having a molecular mass of 3363.2 Dalton and a Molecular formula of C148H244N42O47.

Formulation

The protein was lyophilized with no additives.

Purity

Greater than 93.3% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

Biological Activity (based on net peptide) was found to be 6695.2 IU/mg.

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Introduction
Elcatonin is a Calcitonin derivative which is transformed from eel´s calcitonin by changing the S-S bond into the stable C-N bond. It inhibits the absorption and autolysis of bones, thus leads to blood calcium descending. In addition, it inhibits the bone salts dissolving and transferring and promotes the excretion of calcium and phosphorus in urine. Meanwhile, it inhibits renal tubules reabsorbing calcium, phosphorus and sodium and keeps blood calcium at normal level. It is mainly used for remitting or eliminating the pain caused by Osteoporosis.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Elcatonin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Elcatonin should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Elcatonin in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
Ser-Asn-Leu-Ser-Thr-Asu-Val-Leu-Gly-Lys-Leu-Ser-Gln-Glu-Leu-His-Lys-Leu-Gln-Thr-Tyr-Pro-Arg-Thr-Asn-Val-Gly-Ala-Gly-Thr-Pro-NH2.

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.

Description:

Endothelial Differentiation-Related Factor 1 Human Recombinant

EDF-1, MBF1, Multiprotein-bridging factor 1.

Product # :

PRO-494

Price :

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Shipped with Ice Packs

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Description

EDF1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 156 amino acids (1-148 a.a.) and having a molecular mass of 17.4 kDa. The EDF1 is fused to 8 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
EDF1 controls endothelial cell differentiation. EDF1 has a role as a bridging protein that interconnects regulatory proteins and the basal transcriptional machinery, thus modulating the transcription of genes that take part in endothelial differentiation. EDF1 binds calmodulin through its IQ domain and controls nitric oxide synthase activity via calmodulin sequestration in the cytoplasm. EDF1 is localized in adult liver, heart, adipose tissues, intestine and pancreas.
Synonyms
EDF-1, MBF1, Multiprotein-bridging factor 1.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze thaw cycles.
Amino Acid Sequence
MAESDWDTVT VLRKKGPTAA QAKSKQAILA AQRRGEDVET SKKWAAGQNK QHSITKNTAK LDRETEELHH DRVTLEVGKV IQQGRQSKGL TQKDLATKIN EKPQVIADYE SGRAIPNNQV LGKIERAIGL KLRGKDIGKP IEKGPRAKLE 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.

Description:

Eukaryotic Translation Initiation Factor 4E Human Recombinant

CBP, EIF4E1, EIF4EL1, EIF4F.

Product # :

PRO-530

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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Description

EIF4E Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 237 amino acids (1-217 a.a.) and having a molecular weight of 27.2kDa. The EIF4E is fused to a 20 aa His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The EIF4E 0.5mg/ml protein solution contains 20mM Tris-HCl, pH-8, and 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
EIF4E is part of the eukaryotic initiation factor 4 families, controls translation of maternal mRNAs in early embryos before the onset of zygotic transcription. EIF4E identifies and binds to the 7 methyl GTP cap structure of eukaryotic mRNAs, thus modulates the initiation of translation. EIF4E enables ribosome binding by inducing the unwinding of the mRNAs secondary structures.
Synonyms
CBP, EIF4E1, EIF4EL1, EIF4F.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MATVEPETTP TPNPPTTEEE KTESNQEVAN PEHYIKHPLQ NRWALWFFKN DKSKTWQANL RLISKFDTVE
DFWALYNHIQ LSSNLMPGCD YSLFKDGIEP MWEDEKNKRG GRWLITLNKQ QRRSDLDRFW LETLLCLIGE SFDDYSDDVC GAVVNVRAKG
DKIAIWTTEC ENREAVTHIG RVYKERLGLP PKIVIGYQSH ADTATKSGST TKNRFVV.

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.

Description:

ERGIC And Golgi 3 Human Recombinant

ERGIC And Golgi 3,Serologically Defined Breast Cancer Antigen NY-BR-84, Serologically Defined Breast Cancer Antigen 84, C20orf47, SDBCAG84, Erv46, Endoplasmic Reticulum-Golgi Intermediate Compartment Protein 3, Endoplasmic Reticulum-Localized Protein ERp43,Chromosome 20 Open Reading Frame 47,DJ477O4.2, NY-BR-84, PRO0989,CGI-54, ERGIC3.

Product # :

PRO-2158

Price :

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Shipping Method :

Shipped with Ice Packs

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Description

ERGIC3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 318 amino acids (47-341 a.a) and having a molecular mass of 36.1kDa.ERGIC3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

ERGIC3 protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
ERGIC And Golgi 3, also known as ERGIC3 is a member of the ERGIC family and interacts with ERGIC1/ERGIC32. ERGIC3 takes part in the transport between endoplasmic reticulum and Golgi. One of the diseases which is associated with ERGIC3 is Breast Cancer.
Synonyms
ERGIC And Golgi 3,Serologically Defined Breast Cancer Antigen NY-BR-84, Serologically Defined Breast Cancer Antigen 84, C20orf47, SDBCAG84, Erv46, Endoplasmic Reticulum-Golgi Intermediate Compartment Protein 3, Endoplasmic Reticulum-Localized Protein ERp43,Chromosome 20 Open Reading Frame 47,DJ477O4.2, NY-BR-84, PRO0989,CGI-54, ERGIC3.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSQYYLTTE VHPELYVDKS RGDKLKINID VLFPHMPCAY LSIDAMDVAG EQQLDVEHNL FKQRLDKDGI PVSSEAERHE LGKVEVTVFD PDSLDPDRCE SCYGAEAEDI KCCNTCEDVR EAYRRRGWAF KNPDTIEQCR REGFSQKMQE QKNEGCQVYG FLEVNKVAGN FHFAPGKSFQ QSHVHVHDLQ SFGLDNINMT HYIQHLSFGE DYPGIVNPLD HTNVTAPQAS MMFQYFVKVV PTVYMKVDGE VLRTNQFSVT RHEKVANGLL GDQGLPGVFV LYELSPMMVK LTEKHRSF

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.

Description:

Proliferation-associated protein 2G4, Mouse Anti Human

Proliferation-associated protein 2G4, Cell cycle protein p38-2G4 homolog, hG4-1, ErbB3-binding protein 1, PA2G4, EBP1, p38-2G4.

Product # :

ANT-655

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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formulation
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Formulation

1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.

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Introduction
PA2G4 belongs to the peptidase M24C family and functions as an RNA-binding protein involved in cellular proliferation and differentiation processes. PA2G4 is a component of pre-ribosomal ribonucleoprotein complexes, participating in ribosome assembly and regulating the later steps of rRNA processing. Also, PA2G4 interacts with ErbB-3 and may function as a modulator of the ErbB-3 mediated signal transduction pathway by regulating the effects of Neuregulin-1. Furthermore, PA2G4 is a transcriptional co-repressor of androgen receptor-regulated genes and other cell cycle regulatory genes through its interactions with histone deacetylases. PA2G4 is implicated in growth inhibition and the induction of differentiation of human cancer cells. In addition, PA2G4 mediates cap-independent translation of specific viral IRESs (internal ribosomal entry site). PA2G4 associates with 28S, 18S and 5.8S mature rRNAs, several rRNA precursors and probably U3 small nucleolar RNA.
Synonyms
Proliferation-associated protein 2G4, Cell cycle protein p38-2G4 homolog, hG4-1, ErbB3-binding protein 1, PA2G4, EBP1, p38-2G4.
Physical Appearance
Sterile filtered colorless solution.
Immunogen
Anti-human PA2G4 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human PA2G4 protein 1-394 amino acids purified from E. coli.
Ig Subclass
Mouse IgG1 heavy chain and k light chain.
Clone
PAT5E7AT.
Applications
The antibody has been tested by ELISA, Western blot analysis, Flow cytometry and ICC/IF to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.
Type
Mouse Anti Human Monoclonal.
Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
Purification Method
PA2G4 antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.

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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